Albumin Preparations Research Articles

Comparative analysis of purity of human albumin preparations for clinical use

BackgroundAlbumin is the most prevalent plasma protein and serves numerous physiological roles, both in body fluid management and in various other capacities. In many diseases, a deficiency of albumin has been observed, and in certain conditions, albumin substitution has been demonstrated to improve outcome in comparison to plasma expansion using crystalloid or other colloid solutions. The favourable effects of using albumin in patients with liver cirrhosis are likely associated with the non-oncotic functions of albumin. Albumin for clinical use is obtained through fractionation of pooled donor plasma. The production procedures are optimized to ensure pure, chemically uncompromised and native protein. ResultsWe have extensively analysed commercial preparations of human albumin for clinical use from six different providers. Parameters that must correspond to the requirements of international pharmacopoeias were assessed (aluminium, ethanol, sodium, the presence of dimers and oligomers) and found to conform in all cases. In addition, we used for the first time nuclear magnetic resonance (NMR) as an additional analytical approach for investigating in greater depth the quality of a biological remedy gained from human plasma. We applied both 1H NMR and 13C-HSQC for confirming the identity of the albumin preparations, which also conformed in all cases. Moreover, we utilized T2-filtered 1H NMR and 13C-HSQC measurements to identify the presence of small molecules in the preparations. This demonstrated similar patterns of additional substances present, but also unveiled certain differences in purity in the products of the different providers. SignificanceOur analyses confirmed that albumin preparations in clinical use conform to the requirements. We furthermore demonstrate that NMR measurements can provide further depth in identity and purity measurements of biologicals. Despite largely standardized protocols in pharmaceutical albumin production, our in-depth analyses revealed differences in purity. Some samples exhibited lower levels of components other than albumin. We discuss possible causes of these observations and their potential implications for clinical therapy.

Recurrent Massive Hydrothorax in a Patient with Decompensated Liver Cirrhosis

Aim: to demonstrate the need for a detailed differential diagnosis and selection of therapy in a patient with decompensated liver cirrhosis of combined etiology (HCV infection and primary sclerosing cholangitis). Key points. The patient came to the clinic with complaints of shortness of breath with minimal physical activity, abdominal enlargement, swelling of the legs, yellowness of the skin, and severe weakness. The complaints arose two months after suffering from left-sided focal pneumonia. Laboratory tests revealed signs of systemic inflammation, liver failure, and acute kidney injury. According to the results of instrumental studies, massive hydrothorax was noted in the right pleural cavity. The patient underwent a series of thoracentesis, and a total of about four liters of non-inflammatory pleural fluid was evacuated. Differential diagnosis was based on the presence of dyspnea and respiratory failure. The patient received effective antiviral therapy with drugs using an interferon-free regimen. Subsequently, conservative therapy was carried out, against the background of which the symptoms regressed and the patient’s condition improved. Conclusions. Hepatopleural syndrome is a serious complication in patients with decompensated liver cirrhosis, although it does not always appear secondary to massive ascites. To resolve hepatic hydrothorax, it is necessary to carry out diuretic therapy, replacement transfusion therapy with albumin preparations, and if there is a large amount of fluid in the pleural cavities, therapeutic and diagnostic thoracentesis is recommended.

Methods of intrinsic and probe fluorescence in assessment of the effect of therapeutic radiation doses <i>in vitro</i> on the albumin molecule

Objective. To study in vitro the effect of therapeutic doses of radiation on the albumin molecule using intrinsic and probe fluorescence methods. Materials and methods. In order to study radiation-induced changes in serum albumin during in vitro irradiation with therapeutic doses (2 Gy, 40 Gy and 70 Gy), the study was conducted in 2 directions: therapeutic doses of ionizing radiation irradiated a buffer, which was then used to prepare an albumin solution (pre-irradiation of the buffer); therapeutic doses of ionizing radiation irradiated an albumin buffer solution. The presence of structural and functional (conformational) changes in the albumin molecule was judged by changes in the values of intrinsic (λexc=280 nm) and probe (λexc=280nm, λexc=320 nm) fluorescence. Statistical processing of the obtained data was carried out using the program GraphPad Prism 6.0. Results. Irradiation with therapeutic doses of 2 Gy, 40 Gy and 70 Gy causes conformational changes (a statistically significant decrease in fluorescence intensity) in the albumin molecule, both during preliminary irradiation of the buffer solution used later for the preparation of albumin, and during irradiation of the buffer solution of albumin. Conclusions. Quantitative changes in the fluorescence intensity, both intrinsic and probe, differ under different modes of albumin irradiation.

Polycarboxylate functionalized magnetic nanoparticles Fe3O4@SiO2@CS-COOH: Preparation, characterization, and immobilization of bovine serum albumin

Magnetic nanoparticles with increasing superparamagnetism and magnetic targeting have found widespread application in fields such as food and medicine. In this study, polycarboxylated magnetic nanoparticles (Fe3O4@SiO2@CS-COOH) were prepared by surface functionalizing iron tetraoxide (Fe3O4) nanoparticles with ethylenediaminetetraacetic acid (EDTA) as a modifier. The appropriate degree of functionalization modification was obtained by adjusting the EDTA concentration and the ratio of cross-linking agents. The prepared magnetic nanoparticles were analyzed with structural and property characterization. The results showed that the Fe3O4@SiO2@CS-COOH magnetic nanoparticles prepared with 4 % EDTA and cross-linking agents at a molar ratio of 3:4 were uniform in particle size, with an average size of roughly 7 nm, and possessed an abundant carboxylate content (310.8064 μmol/g) and a high magnetization intensity (35.05 emu/g). As a model protein, bovine serum albumin (BSA) was immobilized on the surface of magnetic particles. The largest amount of immobilized protein was 500.4376 mg BSA/g at pH 4.0 and no extra salt ions. According to molecular docking simulations, its immobilization was due to the interaction of amino and carboxyl groups at the Fe3O4@SiO2@CS-COOH/BSA interface. Fe3O4@SiO2@CS-COOH possesses a large number of carboxyl groups, strong protein immobilization, and magnetic responsiveness, which may have potential applications in biomedical and food fields.

Comparative analysis of quality attributes of a human albumin preparation with a modified stabilising composition

Scientific relevance. The national and international human albumin preparations registered in the Russian Federation mainly differ in their excipient compositions. While all the international preparations of human albumin contain a mixture of sodium caprylate and N-acetyl-DL-tryptophan, the Russian ones contain only sodium caprylate. However, albumin stabilisation with sodium caprylate at high concentrations affects the ligand-binding properties of albumin. For this reason, as well as to achieve storage stability not only at temperatures of 2 °C to 8 °C but also at room temperature, most international manufacturers have reduced the sodium caprylate content in albumin preparations and added N-acetyl-DL-tryptophan. This demonstrates the relevance of studying the quality of a new Russian human albumin preparation with a modified stabilising composition, including both sodium caprylate and N-acetyl-DL-tryptophan.Aim. The study aimed at comparing several quality attributes of the human albumin preparation with a modified stabilising composition with those of imported human albumin preparations.Materials and methods. The human albumin preparation with a modified stabilising composition was manufactured by fractionation from donor plasma meeting the requirements of monograph FS.3.3.2.0001.19 of the State Pharmacopoeia of the Russian Federation edition XIV. The quality control was in line with the monograph on human albumin (FS.3.3.2.0006.18), and statistical analysis was conducted in Microsoft Excel in accordance with the general chapter on statistical analysis (OFS.1.1.0013.15).Results. The study preparation complied with the requirements specified in monograph FS.3.3.2.0006.18. All the manufactured batches were clear, thermostable, sterile, and non-pyrogenic. The prekallikrein activator levels were low (below 1 IU/mL). The aluminium content varied from 30.36±10.39 µg/L to 50.22±6.94 µg/L. The study preparation contained sodium ions at a concentration from 127.44±10.46 mmol/L to 145.59±7.32 mmol/L and less than 0.01 mmol/g of potassium ions. The osmolarity exceeded 240 mOsm/L. The content of α- and β-globulins ranged from 1.79±0.06% to 2.24±0.20%. The study preparation had a pH level of 6.9 to 7.2. The concentrations of polymers and aggregates did not exceed 0.5%.Conclusions. The quality attributes studied suggest that the human albumin preparation with a modified stabilising composition is comparable to its international counterparts and that it meets Russian and European pharmacopoeial standards.

Utilization of ultrasound and glycation to improve functional properties and encapsulated efficiency of proteins in anthocyanins.

The purpose of this study is to explore the optimal conditions for the preparation of bovine serum albumin (BSA)/casein (CA)-dextran (DEX) conjugates by ultrasonic pretreatment combined with glycation (U-G treatment). When BSA and CA were treated with ultrasound (40% amplitude, 10min), the grafting degree increased 10.57% and 6.05%, respectively. Structural analysis revealed that ultrasonic pretreatment changed the secondary structure, further affected functional properties of proteins. After U-G treatment, the solubility and thermal stability of BSA and CA was significantly increased, and the foaming and emulsifying capacity of proteins were also changed. Moreover, ultrasonic pretreatment and glycation exhibited a greater impact on BSA characterized with highly helical structure. Complexes fabricated by U-G-BSA/CA and carboxymethyl cellulose (CMC) exhibited protection on anthocyanins (ACNs), delaying the thermal degradation of ACNs. In conclusion, the protein conjugates treated by ultrasonic pretreatment combined with glycation have excellent functionality and are potential carrier materials.

Preparation of eicosavalent triazolylsialoside-conjugated human serum albumin as a dual hemagglutinin/neuraminidase inhibitor and virion adsorbent for the prevention of influenza infection

A triazolylsialoside-human serum albumin conjugate was prepared as a multivalent hemagglutinin and neuraminidase inhibitor using a di-(N-succinimidyl) adipate strategy. Matrix-Assisted Laser Desorption/Ionization-Time of Flight-Mass Spectrometry (MALDI-TOF-MS) indicated that five tetravalent sialyl galactosides were grafted onto the protein backbone resulting in an eicosavalent triazolylsialoside-protein complex. Compared with monomeric sialic acid, molecular interaction studies showed that the synthetic pseudo-glycoprotein bound tightly not only to hemagglutinin (HA)/neuraminidase (NA) but also to mutated drug-resistant NA on the surface of the influenza virus with a dissociation constant (KD) in the 1 μM range, attributed to the cluster effect. Moreover, this glycoconjugate exhibited potent antiviral activity against a broad spectrum of virus strains and showed no cytotoxicity towards Human Umbilical Vein Endothelial Cells (HUVECs) and Madin-Darby canine kidney (MDCK) cells at high concentrations. Further mechanistic studies demonstrated this multivalent sialyl conjugate showed strong capture and trapping of influenza virions, thus disrupting the ability of the influenza virus to infect host cells. This research lays the experimental foundation for the development of new antiviral agents based on multivalent sialic acid-protein conjugates.

QUALITY EVALUATION OF PHARMACEUTICAL HUMAN SERUM ALBUMIN PREPARATIONS AVAILABLE IN PHARMACIES IN ADEN GOVERNORATE - YEMEN

Human serum albumin(HAS) is important for the body, as it performs a set of functions such as maintaining osmotic pressure inside cells, transporting drugs and ions, and others. The fraudulent process of such preparations may lead to the deterioration of the patient's health condition and sometimes death. In the current study, two types of albumin preparations that were not authorized by the Yemeni ministry of health and entered the country through smuggling were studied. The results of the study proved that these preparations were exposed to high temperatures, so that denaturation of HSA, in addition to the oxidation process of the substance N-acetyl-tryptophan. The reverse phase (RP) high-performance liquid chromatography (HPLC) method to assess HSA, a gradient elution (a combination of acetonitrile/water, supplemented with 0.1% (v/v) trifluoroacetic acid) was used to separate samples on a C4 (n-butyl-coated silica) column. Two main peaks were observed at 4.970 and 10.850 min, representing the stabilizer N-acetyl-tryptophan (N-Ac-Trp) and HSA respectively. Validation of the method demonstrated that HSA can be determined in an accurate and precise manner, in a range between 0.1 and 5g/ml, without the interference of matrix ingredients. The limit of detection (LOD) and lower limit of quantification (LLOQ) values were 0.23 and 0.72 g /ml, respectively. The results of the study proved that these preparations do not meet the quality specifications of the World Health Organization, in addition to exposure to temperatures and bad storage leading to oxidation. The results of the analysis of all samples were less than the permissible limit because each sample must contain 10 grams per 50 ml.

The role of human serum albumin in prevention and treatment of Alzheimer’s disease

Alzheimer’s disease (AD) has been and remains the main cause of dementia in aging patients. This neurodegenerative disease belongs to the progressive and socially significant ones. There are several hypotheses for the development of AD: the tau hypothesis, the amyloid cause, the cholinergic cause, the cause of oxidative stress and inflammation. The lack of a generally accepted understanding of the etiology and pathogenesis of AD hinders the development of new effective mechanisms for its treatment and prevention. In 2021, for the first time, a drug for pathogenetic therapy of AD (aducanumab) was approved, which helps to reduce the content of amyloid-β peptide (Aβ) in the brain of patients. Another promising approach to the treatment of AD, aimed at removing Aβ from the patient’s central nervous system, is the impact on human serum albumin (HSA), which carries 90% of Aβ in the blood serum and 40–90% of Aβ in the cerebrospinal fluid. In clinical practice, plasmapheresis has already been tested and shown to be effective with the replacement of one’s own HSA with a purified therapeutic albumin preparation. Another variant of this approach is to enhance the interaction of HSA with Aβ through the action of exogenous and endogenous HSA ligands, such as serotonin, ibuprofen and some unsaturated fatty acids. In vivo studies confirm the association of this group of ligands with the pathogenesis of AD. These substances are well-studied natural metabolites or drugs, which greatly simplifies the development of new methods of therapy and prevention of AD with their use. In general, a new direction of scientific research devoted to the study of HSA as a carrier and depot of Aβ in the blood and cerebrospinal fluid will expand our understanding of Aβ metabolism and its role in the pathogenesis of AD.

Effects of amino acids and albumin administration on albumin metabolism in surgically stressed rats: A basic nutritional study.

Nutrition therapy and administration of albumin preparations are common in postsurgical patients. However, the effects of these interventions on albumin metabolism are unclear. We elucidated the effect of postoperative albumin and/or parenteral nutrition administration on it. Sprague-Dawley rats underwent surgery involving intestinal rubbing followed by intestinal exposure. Subsequently, they were administered experimental solutions for 48 h, their blood samples were collected at 24 and 48 h, and livers were excised at 48 h. Based on experimental solutions, rats were divided into five groups: non-surgical (Non-surg); glucose and electrolyte solution (GE); amino acid, glucose, and electrolyte solution (AGE); GE + rat serum albumin (Alb) (GE + Alb); and AGE + Alb. Their plasma albumin concentrations; albumin fractional synthesis rate (ALB FSR); mercaptoalbumin/total albumin ratio (MA ratio); and messenger RNA (mRNA) expressions of albumin and hepatocyte nuclear factor-1 (HNF-1) in the liver were measured. The GE and AGE groups showed significant decline in albumin concentrations. ALB FSR was significantly enhanced in the AGE group compared with the GE group. The mRNA expression of albumin was similar to ALB FSR in all groups and that of HNF-1 was significantly decreased in the GE + Alb and AGE + Alb groups compared with the Non-surg group. The MA ratio in the AGE group was similar to the Non-surg group. The administration of amino acids comprising parenteral nutrition after surgery augmented ALB FSR and maintained the MA ratio only without simultaneous albumin administration.

Cell-free and concentrated ascites reinfusion therapy versus large-volume paracentesis for the treatment of cirrhotic patients with refractory ascites: A multicenter prospective observational study.

Cell-free and concentrated ascites reinfusion therapy (CART) and large-volume paracentesis (LVP) with albumin infusion are useful for managing refractory ascites (RA). However, it remains unclear which therapy is more effective in patients with cirrhosis with RA. From June 2018 to March 2022, 25 patients with RA treated with CART or LVP with albumin infusion were enrolled in this multicenter prospective observational study to investigate the number of abdominal paracenteses, albumin preparations used, and drainage volume during an 8-week observation period. Among all patients at entry (median age, 63years; 52% men; 60% Child-Pugh B and 40% Child-Pugh C), 92% were treated with furosemide (median, 20mg/day), 92% with spironolactone (25mg/day), and all with tolvaptan (7.5mg/day). Patients with RA had a poor health-related quality of life (HRQOL) and prominent ascites-related symptoms. Four of the 20 eligible patients were treated with CART, 11 with LVP with albumin infusion, and five with their combination. The median number of paracenteses, total drainage volume, and albumin infusions were 1.5, 7.4L, and 0, respectively, in the CART group; 5.0, 22.0L, and 5.0, respectively, in the LVP group; and 5.0, 30.0L, and 5.0, respectively in their combination group. The treatment effects did not differ significantly among the three groups regarding weight loss, liver function, renal function, electrolytes, and HRQOL. However, patients treated with CART had fewer paracenteses and albumin infusions than those treated with LVP. CART and LVP have comparable therapeutic efficacy for RA in patients with cirrhosis.

Nanoencapsulation as a Promising Platform for the Delivery of the Morin-Cu(II) Complex: Antibacterial and Anticancer Potential.

Nanoencapsulation has emerged as a promising approach for the effective delivery of poorly aqueous soluble compounds. The current study focuses on the preparation of human serum albumin (HSA)-based nanoparticles (NPs) and poly lactic-co-glycolic acid (PLGA)-based nanoparticles for effective delivery of the morin-Cu(II) complex. The NPs were analyzed based on different parameters such as particle size, surface charge, morphology, encapsulation efficiency, and in vitro release properties. The average particle sizes were found to be 214 ± 6 nm for Mor-Cu-HSA-NPs and 185 ± 7.5 nm for Mor-Cu-PLGA-NPs. The release of the morin-Cu(II) complex from both the NPs (Mor-Cu-HSA-NPs and Mor-Cu-PLGA-NPs) followed a biphasic behavior, which comprises an early burst release followed by a sustained and controlled release. The resulting NPs also exhibit free radical scavenging activity confirmed by a standard antioxidant assay. The antibacterial activities of the NPs were investigated using a disk diffusion technique, and it was observed that both the NPs showed better antibacterial activity than morin and the morin-Cu(II) complex. The anticancer activities of the prepared NPs were examined on MDA-MB-468 breast cancer cell lines using a cytotoxicity assay, and the mode of cell death was visualized using fluorescence microscopy. Our results revealed that NPs kill the cancer cells with greater efficiency than free morin and the morin-Cu(II) complex. Thus, both HSA-based NPs and PLGA-based NPs can act as promising delivery systems for the morin-Cu(II) complex and can be utilized for further biomedical applications.

Albumin-Based Nanoparticles for the Delivery of Doxorubicin in Breast Cancer.

Simple SummaryDoxorubicin (Dox) is a chemotherapeutic agent usually employed for the treatment of breast cancer. However, its use is limited because of the toxicities associated, and hence a proper delivery vehicle is necessary. In this sense, albumin-based nanocarriers are in the limelight for the successful delivery of chemotherapeutics because of safety, biocompatibility, and specific cancer-targeting properties. Herein, we have developed a nanocarrier system based on albumin, which selectively affects the tumor cells, and hence can revolutionize breast cancer therapy. The developed nanoparticles could be further used for the delivery of other hydrophobic drugs like SN38, which broadens the use of this system in the treatment of breast cancer.Albumin-based nanoparticles are an emerging platform for the delivery of various chemotherapeutics because of their biocompatibility, safety, and ease of surface modification for specific targeting. The most widely used method for the preparation of albumin nanoparticles is by desolvation process using glutaraldehyde (GLU) as a cross-linker. However, limitations of GLU like toxicity and interaction with drugs force the need for alternative cross-linkers. In the present study, several cross-linking systems were evaluated for the preparation of Bovine Serum Albumin (BSA) nanoparticles (ABNs) encapsulating Doxorubicin (Dox). Based on the results obtained from morphological characterization, in vitro release, and therapeutic efficacy in cells, N-succinimidyl 3-(2-pyridyldithio) propionate (SPDP)-modified ABNs (ABN-SPDP) was chosen. Since ABN-SPDP are formed with disulfide linkage, the drug release is facilitated under a highly reducing environment present in the tumor sites. The cytotoxicity studies of those ABN-SPDP were performed in three different breast cell lines, highlighting the mechanism of cell death. The Dox-encapsulated ABN-SPDP showed toxicity in both the breast cancer cells (MCF-7 and MDA-MB-231), but, remarkably, a negligible effect was observed in non-tumoral MCF-10A cells. In addition to the hydrophilic Dox, this system could be used as a carrier for hydrophobic drugs like SN38. The system could be employed for the preparation of nanoparticles based on human serum albumin (HSA), which further enhances the feasibility of this system for clinical use. Hence, the albumin nanoparticles developed herein present an excellent potential for delivering various drugs in cancer therapy.

Characterization of sonochemically prepared human serum albumin nanocapsules using different plant oils as core component for targeted drug delivery

The focus of this study is the preparation of proteinaceous human serum albumin (HSA) nanocapsules with biocompatible plant oil cores avoiding toxic cross-linker and noxious non-aqueous liquids. The sonochemical preparation of HSA capsules with different plant oils yields particles with narrow size distribution forming suspensions stable for at least 14 days and enabling long-term storage by freezing. Furthermore, wheat germ agglutinin (WGA) as a targeting molecule was successfully embedded into the proteinaceous particle shell at a molar ratio of 7:1 (HSA/WGA). As urothelial cell binding studies revealed up to 55% higher cell binding potential of WGA-grafted particles than those without a targeter, targeted protein nanocapsules represent the first step towards new and innovative formulations.

Исследование Радиационной Безопасности gри Приготовлении 188Re-меченных Микросфер Альбумина lля Лечения Резистентных Синовитов

The article is written about studying of radiation safety of 188Re-labeled microspheres of albumin preparation (hand mode) for treatment of resistant synovitis. The study material was a radiopharmaceutical based on albumin microspheres 5 –10 µm with rhenium-188 for treatment of resistant synovitis. The studying has led to conclusion the number of radiopharmaceutical portions prepared by one operator should not exceed 70 times a year, which will ensure that the main limits of equivalent doses to hands and skin with a reserve factor of 2 (250 μSv/h) are not exceeded. Protective equipment should be used to reduce doses to hands, as the most critical to operator's body part irradiation.

Facile and scalable preparation of bovine serum albumin stabilized cobalt sulfide nanostructures with various morphologies

We present a protein-assisted method for the facile and scalable synthesis of Cobalt sulfide (CoS) nanostructures with various morphologies using bovine serum albumin (BSA) as a stabilizing agent. The CoS samples prepared from 10:1 volume ratio of Cobalt (Co):Sulfur (S) and 1:10 volume ratio of Co:S at 0.01% w/v amount of BSA shows 3D flowers with an average diameter of 510 nm and hollow spheres about 900 nm in average diameter, respectively. The CoS samples prepared from 0.01, 0.1 and 0.5% w/v amounts of BSA at 1:1 volume ratio of Co:S shows nanosheet based porous clusters, nanosheet based partially porous clusters and aggregated spheres, respectively. Fourier transform infrared spectroscopy study confirms that the obtained BSA stabilized CoS nanostructures are stabilized by hydroxyl and amine groups present in the BSA molecules.

Preparation of Heat-Denatured Macroaggregated Albumin for Biomedical Applications Using a Microfluidics Platform.

Albumin is widely used in pharmaceutical applications to alter the pharmacokinetic profile, improve efficacy, or decrease the toxicity of active compounds. Various drug delivery systems using albumin have been reported, including microparticles. Macroaggregated albumin (MAA) is one of the more common forms of albumin microparticles, which is predominately used for lung perfusion imaging when labeled with radionuclide technetium-99m (99mTc). These microparticles are formed by heat-denaturing albumin in a bulk solution, making it very challenging to control the size and dispersity of the preparations (coefficient of variation, CV, ∼50%). In this work, we developed an integrated microfluidics platform to create more tunable and precise MAA particles, the so-called microfluidic-MAA (M2A2). The microfluidic chips, prepared using off-stoichiometry thiol-ene chemistry, consist of a flow-focusing region followed by an extended and water-heated curing channel (85 °C). M2A2 particles with diameters between 70 and 300 μm with CVs between 10 and 20% were reliably prepared by adjusting the flow rates of the dispersed and continuous phases. To demonstrate the pharmaceutical utility of M2A2, particles were labeled with indium-111 (111In) and their distribution was assessed in healthy mice using nuclear imaging. 111In-M2A2 behaved similarly to 99mTc-MAA, with lung uptake predominately observed early on followed by clearance over time by the reticuloendothelial and renal systems. Our microfluidic chip represents an elegant and controllable method to prepare albumin microparticles for biomedical applications.

Fatty acids present in commercial albumin preparations differentially affect development of murine embryos before and during implantation

To characterize fatty acid (FA) profile of commercially available albumin products and determine their effect on embryonic development. Research study. Private research facility. Outbred mice aged 4-8 weeks. Gas chromatography-mass spectrometry was used to quantify the FA content of 15 commercial albumins. Embryos were produced in media containing different albumin products, with or without carnitine or exogenous FA supplementation, to determine their effect on embryo development invitro. Total micrograms of FA per milligram of albumin for the 15 albumin products, blastocyst development, cell number, allocation to the trophectoderm (TE) or inner cell mass (ICM), and evaluation of morphology during implantation. The albumin products contained 0.07-16.77 μg total FA/mg albumin. Compared to media with with >1.4 μg FA/mg albumin, media with <0.5 μg FA/mg albumin supported improved blastocyst development, and addition of carnitine mitigated this difference. Addition of palmitoleic acid or oleic acid individually did not improve blastocyst development and decreased ICM:TE ratio. However, in the presence of carnitine, there was improved blastocyst development and maintenance of the ICM:TE ratio. Embryos cultured inVitrolife human serum albumin with supplementation of carnitine, palmitoleic acid, and oleic acid were more likely to develop cells positive for POU5F1 in an extended embryo culture than embryos cultured in Origio serum protein substitute. Commercial albumin products contain FAs, which vary in abundance. These FAs have different effects on embryo development and quality before and during the implantation stage. Several of these albumin preparations are routinely used for human-assisted reproductive technologies; therefore, serious consideration is warranted when selecting a product for clinical use.

Albumin and functionalized albumin nanoparticles: production strategies, characterization, and target indications.

The inherent properties of albumin facilitate its effective use as a raw material to prepare a nanosized drug delivery vehicles. Because of the enhanced surface area, biocompatibility, and extended half-life of albumin nanoparticles, a number of drugs have been incorporated in albumin matrices in recent years. Furthermore, its ability to be conjugated to various receptor ligands makes albumin an ideal candidate for the increased delivery of drugs to specific sites. The present review provides an in-depth discussion of production strategies for the preparation of albumin and conjugated albumin nanoparticles and for the targeting of these formulations to specific organs and cancer cells. This review also provides insights into drug loading, release patterns, and cytotoxicity of various drug-loaded albumin nanoparticles.

Optimization of the Preparation and Characterization of Tannylated-Albumin Nanoagents

We optimized the preparation of tannylated-human serum albumin (TA-HSA) nanoagents including indocyanine green (ICG) and lobeglitazone (Lobe)-loaded complexes by simple mixing and characterized them. We set the optimal pH at 5 and the optimal weight ratio of [TA]/[HSA] at 1.5 when considering the redispersion of the prepared suspensions in PBS (pH 7.4) and incubation at 37 ·C for the preparation of ICG and/or Lobe-loaded TA-HSA complexes. The immobilization of methoxy polyethylene glycol (mPEG) molecules on TA-HSA-ICG complexes significantly reduces the mean and Z-average sizes of these complexes from the microscale to the nanoscale. Moreover, the use of ICG increases the drug loading efficiency when preparing mPEG-TA-HSA-ICG/Lobe.