Gelatin Research Articles

Bio-sourced flexible supramolecular glasses for dynamic and full-color phosphorescence

Glass, a diverse family of amorphous materials, has significantly advanced human society across various fields. The demand for flexible ultrathin glass, driven by modern optical displays and portable optoelectronics, presents challenges in energy consumption, fabrication complexity, and recycling. Here, we demonstrate flexibility and full-color luminescence in large-scale ultrathin glasses derived from readily available natural resources, specifically egg albumen (EA) and gelatin (GEL), via an evaporation-driven self-assembly process. The dynamic crosslinked networks formed through hydrogen bonding between EA and GEL impart both high hardness and flexibility to the glasses, with hardness and flexural strength values comparable to state-of-the-art inorganic and organic glasses. Additionally, the EA–GEL-based glasses exhibit excitation-dependent and time-gated chiral ultralong phosphorescence with color from blue and red, and a lifetime of up to 180.4 ms. With their easy processability and full-color emission, these biogenic glasses can be fabricated into anti-counterfeiting patterns and optical information codes.

Effect of Oral Administration of Collagen Peptide OG-5 on Advanced Atherosclerosis Development in ApoE−/− Mice

Background/Objectives: Atherosclerosis is a chronic inflammatory disease of the arterial wall, which involves multiple cell types. Peptide OG-5 is identified from collagen hydrolysates derived from Salmo salar and exhibits an inhibitory effect on early atherosclerosis. The primary objective of this study was to investigate the impact of OG-5 on advanced atherosclerotic lesions as well as its stability during absorption. Methods: In this study, the ApoE-/- mice were employed to establish advanced atherosclerosis model to investigate the treatment effect of peptide OG-5. Results: The results showed that oral administration of OG-5 at a dosage of 150 mg/kg bw resulted in a 30% reduction in the aortic plaque formation area in ApoE−/− mice with few bleeding risks. Specifically, intervention with a low dose of OG-5 (50 mg/kg bw), initiated in the early stage of atherosclerosis, continues to provide benefits into the middle and late stages without bleeding risks. Furthermore, treatment of OG-5 increased expression levels of contractile phenotype markers and reduced the accumulation of lipoprotein in VSMCs induced by ox-LDL. Peptide OG-5 could ensure transport across Caco-2 cell monolayers, exhibiting a Papp value of 1.80 × 10−5 cm/s, and exhibited a robust stability in plasma with remaining content >70% after 8 h incubation. In vivo studies revealed that OG-5 reached maximum concentration in blood after 120 min. Conclusion: The present results demonstrate the potential efficacy of peptide OG-5 as a promising agent for intervention in anti-atherogenesis strategies.

Dual drug delivery systems based on natural and synthetic polymer particles for isoniazid and rifampicin vehiculization

AbstractThe purpose of this work is the design and characterization of novel systems based on micro and nanoparticles prepared from poly(lactic‐co‐glycolic) acid (PLGA), chitosan (CHT) and gelatin (GEL) for compartmentalization and dual release of rifampicin and isoniazid. The emulsion/evaporation method is employed for the preparation of PLGA based microparticles and nanoparticles. CHT and GEL are used for the preparation of microparticles by spray‐drying. Entrapment efficiencies are in the range of 35%–73% and 5%–29% for rifampicin and isoniazid in PLGA microparticles, respectively. For isoniazid GEL:CHT particles the entrapment efficiencies are within 82%–100%. Isoniazid shows a complete release at acid condition from GEL:CHT particles, while rifampicin release is maintained from GEL:CHT particles or displays an slightly increase from PLGA particles during buffer conditions. Antimycobacterial activity experiments show that the formulations present the ability to inhibit the bacterial growth in comparison with a control culture without treatment. Rifampicin PLGA and isoniazid GEL:CHT microparticles could be used for the preparation of a dual drug delivery system with each antibiotic in a single particulate compartment. GEL:CHT microparticles containing free isoniazid and rifampicin PLGA nanoparticles are a novel two compartment delivery system.

Maternal Supplementation of Collagen Peptide Chelated Trace Elements Enhances Skeletal Muscle Development in Chicks.

Maternal nutrition plays an important role in regulating the growth and development of offspring. Collagen peptide chelated trace elements (PTE), as a new additive, have been proven to have a positive maternal effect on the intestinal health of offspring, but its effect on the growth anddevelopment is still unclear. This study aimed to investigate the effect of maternal PTE supplementation on the skeletal muscle development of offspring. A total of 270 breeder hens were randomly divided into 3 groups, and fed basal diet (CON), basal diet + 500mg/kg PTE (L-PTE), and 1000mg/kg PTE (H-PTE) for 8weeks. A total of 180 eggs were collected from each group for incubation, and then the hatched male chicks (6 replicates, 12 chicks/replicate) were allocated according to maternal treatment for a 14-day feeding experiment. The results showed that maternal PTE supplementation significantly increased the deposition of iron (Fe), zinc (Zn), and manganese (Mn) in the egg yolk (P < 0.05). In comparison with the CON group, the body weight (days 1 and 14), breast muscle weight (day 14), and muscle fiber density (day 14) of broilers were increased in the L-PTE group (P < 0.05). The serum creatinine (CREA) levels in 1-day-old broilers were reduced in the L-PTE group and H-PTE group(P < 0.05). Additionally, maternal PTE supplementation could upregulate the relative expression level of catalase (CAT) mRNA in breast muscle (P < 0.05). The relative mRNA levels of hemeoxygenase-1 (HO-1) and superoxide dismutase 1(SOD1) in the H-PTE group were significantly upregulated (P < 0.05). Moreover, PTE treatment upregulated the mRNA expression of skeletal muscle development-related genes (Pax7 and MyoG) and the IGF signaling pathway (mTOR, IGF-1R, and IGF-2R) (P < 0.05). In conclusion, maternal PTE supplementation may improve the growth performance and skeletal muscle development of offspring by activating the IGF signaling pathway.

Modulation of biomineralization morphology by phosphorylated collagen peptides: insights into osteogenesis imperfecta pathophysiology.

Osteogenesis imperfecta (OI) is a hereditary skeletal disorder characterized by bone fragility and deformities, primarily attributed to defects in type I collagen, the most abundant structural protein in humans. Multiple phosphorylation sites have been detected within collagen, suggesting that phosphorylation may influence mineralization processes, thereby impacting the development of OI. In this study, we investigated the modulation of biomineralization morphology by phosphorylated collagen peptides mimicking Gly-Ser mutations in osteogenesis imperfecta. A series of collagen peptide sequences, including GPO13S, GPO13pS, GPO12S, GPO12pS, GPO11S, and GPO11pS, were synthesized to explore the role of phosphorylation in peptide stability and its templating effect on biomineralization. The CD results indicated that the phosphorylation of Gly-pSer mutants reduces the stability of collagen peptides. SEM images revealed that phosphorylated peptides acted as templates, guiding the morphology of calcium carbonate into either olive-like or spherical structures, depending on their conformational state of the peptides. Non-phosphorylated peptides maintained a calcite crystal structure. The XRD patterns predominantly exhibited peaks associated with calcite and vaterite for GPO13pS-CaCO3, GPO12pS-CaCO3, and GPO11pS-CaCO3, and peaks associated with calcite for GPO13S-CaCO3, GPO12S-CaCO3, and GPO11S-CaCO3, indicating a transformation of mesocrystals influenced by peptide phosphorylation. Our findings elucidate the crucial role of phosphorylated collagen peptides in mediating biomineralization morphology and polymorph selection, offering insights into the complex pathophysiology of OI.

Investigation of the usefulness of collagen peptide in intramyocardial injection of human iPS cell-derived cardiomyocytes

Abstract Background Injecting human induced pluripotent stem (iPS) cell-derived cardiomyocytes directly into the heart muscle holds promise as a treatment for heart failure. Achieving better engraftment is crucial for maximizing therapeutic effectiveness. Collagen peptide (CP) is a form of hydrolyzed gelatin known for its resistance to solidification. By adjusting its concentration, the viscosity of CP can be easily managed, potentially influencing the retention and engraftment efficiency of transplanted cells. Purpose We investigated the impact of different CP concentrations as a solvent for intramyocardial injection of human iPS cell-derived cardiomyocytes. Methods Initially, we examined the leakage of CP solution from the injection site using chicken meat and ex vivo rat heart. Subsequently, an in vivo experiment was conducted using beating rat myocardium injected with CP solution and Indian ink to assess CP diffusion in dynamic heart tissue. Finally, we performed intramyocardial injections of human iPS cell-derived cardiomyocytes onto a myocardial infarction model in immunosuppressed rats (1.0×107 cells/rat), followed by echocardiographic evaluation of cardiac function four weeks post-transplantation (N=3-6). Results There was less leakage from the injection site at lower CP concentration (10%) compared to higher concentration (20%), particularly in chicken or ex vivo rat heart tissue under static, non-beating conditions (chicken; 10% vs. 20% CP: 3.2±0.7% vs. 11.6±0.8%, P=0.01 / rat heart; 1.5±0.9% vs. 6.8±1.1%, P=0.0072). However, when examining fluid leakage from the cross-section of ex vivo rat hearts, we observed significantly higher leakage, regardless of CP concentration (10% CP: 45.7±2.7%, 20% CP: 59.1±8.1%), suggesting that CP diffusion within myocardial tissues had a greater influence on local retention than leakage from the injection site. Subsequently, in an experiment using beating rat myocardium and Indian ink, we observed significant suppression of diffusion in tissues treated with CP solution, with the 20% concentration showing a tendency to remain at the injection site (0% CP: 24.5±6.2 mm2, 10% CP: 6.9±7.1 mm2, 20% CP: 10.6±3.3 mm2, P=0.005). This indicates that 20% CP, rather than 10% CP, may be more suitable for local retention in tissues experiencing intra-tissue pressure, such as the beating myocardium. Finally, in vivo experiment using a myocardial infarction model of rat, there was no significant difference in left ventricular ejection fraction (LVEF) when cardiomyocytes were transplanted with 10% CP (0％ CP: 56.1±8.9%, 10%CP: 61.9±5.2%, P=0.92). However, there was a trend towards improved LVEF with the 20% CP solution (0% CP: 56.1±8.9%, 20%CP: 68.8±7.9%, P=0.13), Conclusion Twenty-percent CP may be more beneficial for treating myocardial ischemia due to enhanced retention and engraftment of transplanted cardiomyocytes.

Preparation and tissue structure analysis of horse bone collagen peptide

Horse bone is rich in collagen, with a composition similar to that of human collagen. Collagen peptides supply nutrients needed for human growth that act as antioxidants, lower blood pressure. This study explored the extraction of collagen and the preparation of collagen short peptides from Mongolian horse bones. Bones were collected from horses of varying ages, and the collagen content along with calcium salt distribution were observed through staining and imaging analyses. Next, the bones were processed into a powder and then subjected to ultra-high-pressure processing for degreasing. The degreasing conditions were optimised by single-factor and orthogonal tests. Following this, collagen was extracted using an acid-enzymatic method, and its structural characteristics and thermal stability were assessed. The collagen short peptides were extracted from the collagen samples, and the effects of the enzymatic hydrolysis time, temperature, pH, and enzyme amount on the extraction rate were evaluated. Finally, the resulting collagen peptides were analysed for antioxidant activity. In summary, this experiment optimised the extraction conditions for horse bone collagen, demonstrating that the ultra-high-pressure method minimally affects collagen structure, and the extraction rate was high. Hence our method has significant development potential.

Characterization of Trivalently Crosslinked C-Terminal Telopeptide of Type I Collagen (CTX) Species in Human Plasma and Serum Using High-Resolution Mass Spectrometry.

With an aging population, the increased interest in the monitoring of skeletal diseases such as osteoporosis led to significant progress in the discovery and measurement of bone turnover biomarkers since the 2000s. Multiple markers derived from type I collagen, such as CTX, NTX, PINP, and ICTP, have been developed. Extensive efforts have been devoted to characterizing these molecules; however, their complex crosslinked structures have posed significant analytical challenges, and to date, these biomarkers remain poorly characterized. Previous attempts at characterization involved gel-based separation methods and MALDI-TOF analysis on collagen peptides directly extracted from bone. However, using bone powder, which is rich in collagen, does not represent the true structure of the peptides in the biofluids as it was cleaved. In this study, our goal was to characterize plasma and serum CTX for subsequent LC-MS/MS method development. We extracted and characterized type I collagen peptides directly from human plasma and serum using a proteomics workflow that integrates preparative LC, affinity chromatography, and HR-MS. Subsequently, we successfully identified numerous CTX species, providing valuable insights into the characterization of these crucial biomarkers.

Hydroxyprolyl-Glycine in 24 H Urine Shows Higher Correlation with Meat Consumption than Prolyl-Hydroxyproline, a Major Collagen Peptide in Urine and Blood

Background. Urinary collagen peptides, the breakdown products of endogenous collagen, have been used as biomarkers for various diseases. These non-invasive biomarkers are easily measured via mass spectrometry, aiding in diagnostics and therapy effectiveness. Objectives. The objective of this study was to investigate the effects of consuming collagen-containing meat on collagen peptide composition in human blood and urine. Methods. Ten collagen peptides in 24 h urine were quantified. Results. Prolyl-hydroxyproline (Pro-Hyp) was the most abundant peptide. Except for hydroxyprolyl-glycine (Hyp-Gly), levels of other minor collagen peptides showed high correlation coefficients with Pro-Hyp (r = 0.42 vs. r &gt; 0.8). Notably, 24 h urinary Hyp-Gly showed a correlation coefficient of r = 0.72 with meat consumption, significantly higher than the coefficient for Pro-Hyp (r = 0.37). Additionally, the levels of Pro-Hyp and Hyp-Gly in the blood of seven young women participants increased similarly after consuming fish meat, while before ingestion, only negligible amounts of Hyp-Gly were present. To examine which peptides are generated by the degradation of endogenous collagen, mouse skin was cultured. The amount of Pro-Hyp released from the skin was approximately 1000-fold higher than that of Hyp-Gly. Following consumption of collagen-containing meat, both Pro-Hyp and Hyp-Gly are released in blood and excreted into urine, although Pro-Hyp is primarily generated from endogenous collagen even under physiological conditions. Conclusion. Therefore, in 24 h urine samples, the non-negligible fraction of Pro-Hyp is contributed by endogenous collagen, making 24 h urine Hyp-Gly level a potential biomarker for evaluating meat consumption on the day.

Profiling Bioactive Components of Natural Eggshell Membrane (NEM) for Cartilage Protection and Its Protective Effect on Oxidative Stress in Human Chondrocytes

The current study aimed to investigate the physicochemical properties of the natural eggshell membrane (NEM) and its protective effects against H2O2-induced oxidative stress in human chondrocytes (SW-1353). Bioactive components from NEM related to cartilage were profiled, consisting of 1.1 ± 0.07% hyaluronic acid, 1.2 ± 0.25% total sulfated glycosaminoglycans as chondroitin sulfate, 3.1 ± 0.33% collagen, and 54.4 ± 2.40% total protein. Protein was hydrolyzed up to 43.72 ± 0.76% using in vitro gastro–intestinal digestive enzymes. Peptides eluted at 9.58, 12.46, and 14.58 min using nano-LC-ESI-MS were identified as TEW, SWVE, and VYL peptides with an M/Z value of 435.1874, 520.2402, and 394.2336, respectively. Radical scavenging activity of NEM at 10 mg/mL using the ABTS assay was revealed to be 2.1 times higher than that of the positive control. NEM treatment significantly enhanced cellular SOD expression (p &lt; 0.05). Pre-treatment with NEM (0.1, 1, and 10 mg/mL) dose-dependently reduced H2O2-induced ROS levels in SW-1353. Cell live imaging confirmed that NEM pre-treatment led to a significant reduction in apoptosis expression compared to control. Results from the present study suggest that NEM rich in cartilage protective components including hyaluronic acid, collagen, and chondroitin antioxidative peptides could be a potential therapeutic agent for osteoarthritis (OA) by scavenging oxidative stress.

Collagen Type VII (COL7A1) as a Longevity Mediator in Caenorhabditis elegans: Anti-Aging Effects on Healthspan Extension and Skin Collagen Synthesis

Longevity genes and senescence-related signaling proteins are crucial targets in aging research, which aims to enhance the healthy period and quality of life. Identifying these target proteins remains challenging because of the need for precise categorization and validation methods. Our multifaceted approach combined bioinformatics with transcriptomic data to identify collagen as a key element associated with the lifespan of the model organism, Caenorhabditis elegans. By analyzing transcriptomic data from long-lived mutants that involved mechanisms such as antioxidation, dietary restriction, and genetic background, we identified collagen as a common longevity-associated gene. We validated these findings by confirming that collagen peptides positively affect lifespan, thereby strengthening the validity of the target. Further verification through healthspan factors in C. elegans and functional assays in skin fibroblasts provided additional evidence of the role of collagen in organismal aging. Specifically, our study revealed that collagen type VII is a significant target protein for mitigating age-related decline. By validating these findings across different aging models and cell-based studies, we present compelling evidence for the anti-aging effects of collagen type VII, highlighting its potential as a target for promoting healthy aging. This study proposes that collagen not only serves as an indicative marker of organismal longevity across various senescence-related signaling pathways, but also offers a mechanistic understanding of skin degeneration. Consequently, collagen is an effective target for interventions aimed at mitigating skin aging. This study underscores the potential of collagen type VII (bonding collagen T7) as a therapeutic target for enhancing skin health and overall longevity.

A Specific Collagen Hydrolysate Improves Postprandial Glucose Tolerance in Normoglycemic and Prediabetic Mice and in a First Proof of Concept Study in Healthy, Normoglycemic and Prediabetic Humans

ABSTRACTIn response to nutrients, intestinal L‐ and K‐cells naturally secrete glucagon‐like peptide 1 (GLP‐1). GLP‐1 regulates postprandial blood glucose by increasing insulin secretion, slowing down gastric emptying and inducing satiety. A selection of specifically developed collagen hydrolysates was screened for their ability to enhance natural GLP‐1 production in vitro. The best performing hydrolysate, H80 (Nextida GC), was orally administered at different doses to lean, normoglycemic mice and overweight, prediabetic mice. Lean mice were acutely challenged 45 min before an oral glucose load. While daily supplemented for 6 weeks, prediabetic mice were acutely challenged at day 21 and 34. Oral glucose tolerance, plasma insulin and GLP‐1 levels were assessed, and a gastric emptying assay performed in prediabetic mice. H80 significantly lowered the blood glucose response in lean and prediabetic mice, at a 4 g/kg dose (−25% and −36%, respectively), compared to vehicle. In chronically supplemented, prediabetic mice, acute H80 administration slowed down gastric emptying (−60%) after 21 days and increased plasma insulin (+166%) after 35 days of supplementation. H80 increased plasma active GLP‐1 in lean (+217%) and prediabetic (+860%) mice. Overall, the data indicate that the specific collagen hydrolysate, H80, has significant GLP‐1‐mediated effects on oral glucose tolerance in lean and prediabetic mice. Furthermore, effects on postprandial glucose tolerance were evaluated in a small, human, proof of concept study. H80 reduced the postprandial glucose response at a 5 g dose in healthy, normoglycemic and prediabetic participants. Oral supplementation with H80 might thus be a promising strategy to maintain normal glucose tolerance.

The Utilization of Central Composite Design for the Production of Hydrogel Blends for 3D Printing

Central composite design (CCD) is a statistical experimental design technique that utilizes a combination of factorial and axial points to study the effects of multiple variables on a response. This study focused on optimizing hydrogel formulations for 3D printing using CCD. Three biopolymers were selected: sodium alginate (SA), gelatin (GEL), and carboxymethyl cellulose (CMC). The maximum and minimum concentrations of each polymer were established using a Google Scholar search, and CCD was employed to generate various combinations for hydrogel preparation. The hydrogels were characterized in accordance with their swelling degree (SD) in phosphate-buffered saline (PBS) and Dulbecco’s Modified Eagle Medium (DMEM), as well as their printability in 2D and 3D assays. The formulation consisting of 7.5% SA, 7.5% GEL, and 2.5% CMC exhibited the best swelling properties and exceptional printability, surpassing all other tested formulations. This study highlights the effectiveness of design of experiment methodologies in accelerating the development of optimized hydrogel formulations for various applications in 3D printing and suggests avenues for future research to explore their performance in specific biological contexts.

Deciphering the Wound-Healing Potential of Collagen Peptides and the Molecular Mechanisms: A Review.

Collagen peptides have been reported to display various bioactivities and high bioavailability. Recently, increasing evidence has revealed the excellent wound-healing activity of collagen peptides, but their molecular mechanisms remain incompletely elucidated. This review systematically evaluates the therapeutic efficacy of collagen peptides from diverse sources based on various wound models. Furthermore, the structure-activity relationships of collagen peptides and wound-healing mechanisms are discussed and summarized. Characterized by their low molecular weight and abundant imino acids, collagen peptides facilitate efficient absorption by the body to deliver nutrition throughout the wound-healing process. The specific mechanism of collagen peptide for wound healing is mainly through up-regulation of related cytokines and participation in the activation of relevant signaling pathways, such as TGF-β/Smad and PI3K/Akt/mTOR, which can promote cell proliferation, angiogenesis, collagen synthesis and deposition, re-epithelialization, and ECM remodeling, ultimately achieving the effect of wound healing. Collagen peptides can offer a potential therapeutic approach for treating incision and excision wounds, mucosal injuries, burn wounds, and pressure ulcers, improving the efficiency of wound healing by about 10%-30%. The present review contributes to understanding of the wound-healing potential of collagen peptides and the underlying molecular mechanisms.

Applications and Impacts of Edible Coatings on Food Quality

Edible coatings are emerging as a significant trend in the food industry, driven by growing consumer interest in environmental issues, mainly due to concerns about the excessive use of plastics. This study aimed to perform an integrative review to identify the materials used to produce edible films and characterize their applicability for food quality and conservation. For this, the descriptors “edible films” or “edible coatings” and “food quality” or “food preservation” or “food safety” were used in the Science Direct database, resulting in 48 articles selected. Fruits and vegetables are the two food groups most studied with coatings based on hydrocolloids, protein, composite films, and lipids, with a greater emphasis on the positive impacts on their quality and conservation. Animal products have a higher frequency of studied antimicrobial effects. There is a diversity of materials used in coatings: vegetable-based, such as algae, mucilages, and fibers, as well as those of animal origin, such as gelatin and protein hydrolysates. Few studies have addressed sustainability concepts as final characteristics of coatings. In conclusion, edible coatings show promise for the food industry, offering benefits for both food and the environment. However, more studies are needed to fully explore their potential as replacements for conventional plastics, while ensuring safety and regulatory compliance.

Preparation of natural adhesives with high-strength and low temperature fast-curing properties

The development of natural adhesives to substitute petroleum-based products is crucial for sustainable progress. However, the bond strength of most existing natural adhesives still falls short of that of commercially available adhesives and the curing process often demands prolonged high-temperature treatment. Herein, we prepared pure natural adhesives using gelatin (GE), tung oil (TO), and dopamine (DA) as the main raw materials. The shear strength of the adhesive to wood reached up to 6.35 MPa, a significant improvement over most natural wood adhesives reported. Additionally, the tensile strength of the adhesive to wood reached 10.50 MPa, which is comparable to commercially available neoprene-phenolic wood adhesives (9.99 MPa) and cyanoacrylate instant adhesives (9.48 MPa). In addition, the natural adhesive prepared by us exhibits fast curing performance at room temperature and can be fully cured in only 12 min, which is significantly better than the commercially available adhesive. The adhesives prepared in this study also possessed excellent reversible curing properties, antimicrobial properties, low toxicity, and degradability. These characteristics offer new insights for the advancement and dissemination of natural adhesives.

Co-immobilization of lipase and β-galactosidase in gelatin-carboxymethyl cellulose blend films used as an active packaging component

β-Galactosidase and lipase were co-immobilized in polymeric blends of gelatin (GEL) and carboxymethyl cellulose (CMC) synthesized with different ratios of GEL/CMC: A (0GEL:100CMC), B (25GEL:75CMC), C (50GEL:50CMC), D (75GEL:25CMC), E (100GEL:0CMC). The films obtained good electrostatic interaction and a regular and uniform structure. The addition of CMC increased the mechanical resistance of the films, the tensile strength being 35.04 ± 0.10 MPa for A (0GEL:100CMC) films and 19.17 ± 2.44 MPa for E (100GEL:0CMC) films. Thermogravimetry (TG) showed that the addition of the enzyme decreases the thermal stability of the films. Film B (25GEL:75CMC) showed greater affinity with the added enzymes and greater thermal stability, in addition to increasing the crystallinity by up to 5.8 % and forming more transparent films. CMC was the most hydrophilic polymer, with higher moisture content (17.35 ± 1.73 %) and PVA (0.398 ± 0.047 g.mm/h.m2.kPa), higher still after the addition of enzyme (22.91 ± 1.06 % and 1.136 ± 0.087 g.mm/h.m2.kPa). The enzymes showed greater interaction with the bulky groups of CMC and the film with the highest concentration of this polymer was the one that presented the best hydrolysis rate of lactose and triglycerides, enabling the production of films.

Synergetic effect of bioglass and nano montmorillonite on 3D printed nanocomposite of polycaprolactone/gelatin in the fabrication of bone scaffolds

Nowadays, bone injuries and disorders have increased all over the world and can reduce the quality of human life. Bone tissue engineering repair approaches require new biomaterials and methods to construct scaffolds with the required structural properties as well as improved performance. As potential therapeutic strategies in bone tissue engineering, 3D printed scaffolds have been developed. Polycaprolactone/Ceramic composites have attracted considerable attention due to their cytocompatibility, biodegradability, and physical properties. In this study, a 3D printing process was used to create polycaprolactone (PCL)-Gelatin (GEL) scaffolds containing varying concentrations of Bioglass (BG) and Nano Montmorillonite (MMT). This mixture was then loaded into a 3D printer, and the scaffolds were printed layer by layer. After constructing the scaffolds, they were then examined for their physical, chemical, and biological characteristics. Surface appearance was analyzed with a scanning electron microscope (SEM), which revealed that NC increased the diameter of pores from 465 to 480 μm. The elements in the scaffolds were evaluated by EDX analysis, and a uniform dispersion of nano montmorillonite particles was observed. The compressive strength reached 76.43 MPa for PCL/G/35 %MMT/15 %BG scaffold. Also, the rate of water absorption, biodegradability and bioactivity of PCL-GEL scaffolds increased significantly in the presence of NC. According to the MTT cell test results, adding BG and NC increased cell proliferation, adhesion and cell viability to 127.7 %. These findings indicated that the 3D printed PCL/G/35 %MMT/15 %BG scaffold has promising strategies for bone repair applications. Also, polynomial curve fitting shows that scaffold degradability after soaking in PBS can be predicted using the initial weight and soaking time. Adding more variables and data could improve prediction accuracy, reducing the need for experiments and conserving resources.

Comparative Analysis of Collagen Supplementation Forms and Their Effects on Multiple Health Parameters

Collagen, a key structural protein, is essential for maintaining the integrity of connective tissues such as skin, cartilage, tendons, bones. As natural collagen production decreases with age and is further compromised by environmental factors such as UV radiation and poor diet, collagen degradation accelerates, leading to conditions like wrinkles, joint stiffness, and decreased bone density. Collagen supplementation has gained widespread attention as a therapeutic intervention to counteract these effects. This review conducts a comprehensive comparative analysis of various forms of collagen supplementation, including hydrolyzed collagen, undenatured collagen, and gelatin, and their effects on a range of health outcomes. Hydrolyzed collagen, due to enhanced bioavailability, is associated with improvements in skin elasticity, hydration, joint pain relief, and muscle recovery, making it particularly valuable for aging populations and athletes. Undenatured type II collagen, on the other hand, modulates immune responses and shows potential in reducing inflammation and slowing the progression of degenerative joint diseases such as osteoarthritis and rheumatoid arthritis. Gelatin, while less bioavailable than hydrolyzed collagen, still supports skin and joint health when taken in larger quantities. This review also explores emerging evidence of collagen’s beneficial effects on bone density, wound healing, and hair health, with marine-derived collagen showing promise in skin health due to its rapid absorption. Potential adverse effects, including mild gastrointestinal discomfort and rare allergic reactions, are discussed, emphasizing the importance of sourcing high-quality products. Overall, collagen supplementation, particularly hydrolyzed collagen peptides, offers significant therapeutic potential for improving skin, joint, and musculoskeletal health, but further research is required to define optimal dosages, formulations, and long-term safety for various populations.

The Effects of Collagen Peptides as a Dietary Supplement on Muscle Damage Recovery and Fatigue Responses: An Integrative Review.

The oral administration of hydrolyzed collagen peptides is a scientifically validated intervention for enhancing skeletal muscle health and performance. This integrative review consolidates the evidence supporting the use of low molecular weight collagen peptides (2000-3500 daltons) for their superior bioavailability and absorption. Our objective was to review the effects of collagen peptide or hydrolyzed collagen supplementation on muscle damage, recovery, and construction related to physical exercise. A bibliographic search was conducted in major English-language databases, including PubMed/Medline, using terms like "Peptides Collagen and Damage" and "collagen peptides AND Soreness Muscle". This review followed PRISMA guidelines, with bias risk assessed via the PEDro scale. The inclusion criteria were (a) randomized clinical trials, (b) randomized studies in humans with a control or placebo group, (c) studies assessing muscle damage or delayed onset muscle soreness via physiological markers or strength performance tests, and (d) studies using hydrolyzed collagen or collagen peptides. Initially, 752 articles were identified. After applying the inclusion and exclusion criteria, including duplicate removal, eight articles with 286 participants were included. Of these, 130 participants received collagen peptide supplementation, while 171 received a placebo or control. This integrative review supports the potential of collagen peptide supplementation to mitigate muscle stress from acute strenuous resistance training. However, due to the methodological heterogeneity among the studies, further clinical trials are needed to clarify the mechanisms underlying muscle improvement with collagen supplementation.