Changes In Secondary Structure Research Articles

FLT4 gene polymorphisms influence isolated ventricular septal defect predisposition in a Southwest China population

BackgroundVentricular septal defect (VSD) is the most common congenital heart disease. Although a small number of genes associated with VSD have been found, the genetic factors of VSD remain unclear. In this study, we evaluated the association of 10 candidate single nucleotide polymorphisms (SNPs) with isolated VSD in a population from Southwest China.MethodsBased on the results of 34 congenital heart disease whole-exome sequencing and 1000 Genomes databases, 10 candidate SNPs were selected. A total of 618 samples were collected from the population of Southwest China, including 285 VSD samples and 333 normal samples. Ten SNPs in the case group and the control group were identified by SNaPshot genotyping. The chi-square (χ2) test was used to evaluate the relationship between VSD and each candidate SNP. The SNPs that had significant P value in the initial stage were further analysed using linkage disequilibrium, and haplotypes were assessed in 34 congenital heart disease whole-exome sequencing samples using Haploview software. The bins of SNPs that were in very strong linkage disequilibrium were further used to predict haplotypes by Arlequin software. ViennaRNA v2.5.1 predicted the haplotype mRNA secondary structure. We evaluated the correlation between mRNA secondary structure changes and ventricular septal defects.ResultsThe χ2 results showed that the allele frequency of FLT4 rs383985 (P = 0.040) was different between the control group and the case group (P < 0.05). FLT4 rs3736061 (r2 = 1), rs3736062 (r2 = 0.84), rs3736063 (r2 = 0.84) and FLT4 rs383985 were in high linkage disequilibrium (r2 > 0.8). Among them, rs3736061 and rs3736062 SNPs in the FLT4 gene led to synonymous variations of amino acids, but predicting the secondary structure of mRNA might change the secondary structure of mRNA and reduce the free energy.ConclusionsThese findings suggest a possible molecular pathogenesis associated with isolated VSD, which warrants investigation in future studies.

Tannin-on-protein adlayers: Secondary adsorption quantified by quartz crystal microbalance with dissipation monitoring (QCM-D)

The quartz crystal microbalance with dissipation monitoring (QCM-D) technique allows to detect adsorption and mechanical characteristics of protein adsorption layers at solid surfaces, including subsequent secondary adsorption of additional species interacting with the proteins. Here, we study the secondary adsorption of two different classes of tannins - hydrolysable vs. condensed - onto a β-lactoglobulin base layer using QCM-D in a protein/tannin adlayer configuration. Sequential flow experiments of protein solutions, tannin solutions and neat solvent or buffer are used to distinguish reversible from desorption-resistant layer formation, evaluate the viscoelastic characteristics the layers, and map protein/tannin interactions in view of their structural properties and origin. We find that for the majority of tannins, secondary layer structural changes (detected via a change in the dissipation factor) occur before significant mass adsorption (detected via the resonance frequency shift). In contrast, simultaneous onset of structural change and adsorbed mass within an observation window of 100 ms was only found for certain hydrolysable tannins. We use these data to build adsorption maps and group the tannins according to their adlayer properties, providing a physical basis for an improved understanding of the organoleptic perception of tannins and polyphenols, in particular with respect to attributes such as ‘astringency’ and ‘lingering’. Moreover, these maps provide insight into the capacity of different tannins to modify the mechanical properties of protein adsorption layers.

EGCG induced the formation of protein nanofibrils hydrogels with enhanced anti-bacterial activity

The functional properties of the amyloid fibrils could be further improved after physical modification. Simply adding epigallocatechin gallate (EGCG) to ovalbumin amyloid fibrils (OAFs) could successfully drive the formation of hydrogels through the self-assembly of hybrid supermolecules, however the functional properties of amyloid fibrils as well as the underlying formation mechanisms have not been well revealed. In present study, the rheological properties, thermal stability, and morphology of the resulting OAFs hydrogels were investigated, and the secondary structural changes of the proteins in OAFs hydrogels was analyzed. The results showed that the addition of EGCG would affect the diameter of OAFs, mainly as the concentration of EGCG increased from 0.1% to 2%, the diameter of OAFs increased from 3 nm to 5.5 nm. In addition, when the EGCG concentration increased from 0.1% to 0.5%, the content of β-sheet structure increased from 24.3% to 43.7%. Moreover, the OAFs hydrogels exhibited good viscoelasticity and heat resistance, as well as displayed good antioxidant activity and strong anti-bacterial activity against both Gram-negative and Gram-positive bacteria. The present study might provide a theoretical basis for antimicrobial food packaging based on animal amyloid fibrils hydrogels.

Calcium ions do not influence the Aβ(25–35) triggered morphological changes of lipid membranes

We have studied the effect of calcium ions (Ca2+) at various concentrations on the structure of lipid vesicles in the presence of amyloid-beta peptide Aβ(25–35). In particular, we have investigated the influence of calcium ions on the formation of recently documented bicelle-like structures (BLSs) emerged as a result of Aβ(25–35) triggered membrane disintegration. First, we have shown by using small-angle X-ray and neutron scattering that peptide molecules rigidify the lipid bilayer of gel phase DPPC unilamellar vesicles (ULVs), while addition of the calcium ions to the system hinders this effect of Aβ(25–35). Secondly, the Aβ(25–35) demonstrates a critical peptide concentration at which the BLSs reorganize from ULVs due to heating and cooling the samples through the lipid main phase transition temperature (Tm). However, addition of calcium ions does not affect noticeably the Aβ-induced formation of BLSs and their structural parameters, though the changes in peptide's secondary structure, e.g. the increased α-helix fraction, has been registered by circular dichroism spectroscopy. Finally, according to 31P nuclear magnetic resonance (NMR) measurements, calcium ions do not affect the lipid-peptide arrangement in BLSs and their ability to align in the magnetic field of NMR spectrometer. The influences of various concentrations of calcium ions on the lipid-peptide interactions may prove biologically important because their local concentrations vary widely in in-vivo conditions. In the present work, calcium ions were investigated as a possible tool aimed at regulating the lipid-peptide interactions that demonstrated the disruptive effect of Aβ(25–35) on lipid membranes.

Synthesis and evaluation of Maillard conjugates for encapsulation and controlled delivery of quercetin under simulated gastrointestinal tract conditions

AbstractEncapsulation of bioactive molecules for therapeutic use is gaining great interest in the scientific community. Several encapsulation methodologies have been evaluated, sacrificing, in some cases, either encapsulation efficiency or compound integrity. Our work developed Maillard conjugates (MCs) based on the whey protein (WP)‐Maltodextrin (MD) interaction to encapsulate quercetin by freeze‐drying. The WP:MD ratio used (1:2 or 1:3) yielded the formation of MCs, demonstrated by an increased browning index and changes in the protein secondary structure. Freeze‐drying showed high encapsulation efficiency, reaching 87.65% and 84.72% in treatments loaded with 3.3 mg quercetin/g MCs. Quercetin‐loaded MCs showed spherical‐shape (4–10 μm) and a negative charge, suggesting colloidal stability. Moreover, in vitro tests demonstrated a sustained release of quercetin throughout the oral, gastric, and intestinal phases, highlighting the MCs efficacy as bioactive delivery systems. This work provides useful information to design bioactive compound delivery systems for food and pharmaceutical applications.

Mechanism understanding of PIKfyve inhibitor YM201636 with human serum albumin: Insights from molecular modeling and multiple spectroscopic techniques.

YM201636 is the potent PIKfyve inhibitor that is being actively investigated for liver cancer efficacy. In this study, computer simulations and experiments were conducted to investigate the interaction mechanism between YM201636 and the transport protein HSA. Results indicated that YM201636 is stably bound between the subdomains IIA and IIIA of HSA, supported by site marker displacement experiments. YM201636 quenched the endogenous fluorescence of HSA by static quenching since a decrease in quenching constants was observed from 7.74 to 2.39 × 104 M-1. UV-vis and time-resolved fluorescence spectroscopy confirmed the YM201636-HSA complex formation and this binding followed a static mechanism. Thermodynamic parameters ΔG, ΔH, and ΔS obtained negative values suggesting the binding was a spontaneous process driven by Van der Waals interactions and hydrogen binding. Binding constants ranged between 5.71 and 0.33 × 104 M-1, which demonstrated a moderately strong affinity of YM201636 to HSA. CD, synchronous, and 3D fluorescence spectroscopy revealed that YM201636 showed a slight change in secondary structure. The increase of Kapp and a decrease of PSH with YM201636 addition showed that YM201636 changed the surface hydrophobicity of HSA. The research provides reasonable models helping us further understand the transportation and distribution of YM201636 when it absorbs into the blood circulatory system.

UPC2 mutations and development of azole resistance in Candida albicans hospital isolates from Lebanon

ObjectiveThis study evaluated the role of Upc2 in the development of azole resistance in Candida albicans isolates from Lebanese hospitalized patients and determined a correlation between resistance and virulence. MethodsThe UPC2 gene which codes for an ergosterol biosynthesis regulator was sequenced and analyzed in two azole resistant and one azole susceptible C. albicans isolates. An amino acid substitution screening was carried out on Upc2 with a focus on its ligand binding domain (LBD) known to interact with ergosterol. Then, Upc2 protein secondary structure prediction and homology modeling were conducted, followed by total plasma membrane ergosterol and cell wall chitin quantifications. For virulence, mouse models of systemic infection were generated and an agar adhesion and invasion test was performed. ResultsAzole resistant isolates harbored novel amino acid substitutions in the LBD of Upc2 and changes in protein secondary structures were observed. In addition, these isolates exhibited a significant increase in plasma membrane ergosterol content. Resistance and virulence were inversely correlated while increased cell wall chitin concentration does not seem to be linked to resistance since even though we observed an increase in chitin concentration, it was not statistically significant. ConclusionThe azole resistant C. albicans isolates harbored novel amino acid substitutions in the LBD of Upc2 which is speculated to induce an increase in plasma membrane ergosterol content, preventing the binding of azoles to their target, resulting in resistance.

Effects of non-covalently bound polyphenols/vitamins on the structure and functional characteristics of egg yolk powder

The egg yolk powder (EYP) was modified in this study by incorporating the tea polyphenols (TP), rosemary extract (RE), curcumin (CC), ascorbic acid (AA), and vitamin E (VE) to create the complex of polyphenols/vitamins-EYP. The structure, flavor, and emulsification properties of the complex were investigated. The results demonstrated that the addition of these five substances enhanced the flavor of EYP. Among them, VEP (EYP modified by VE) exhibited the flavor profile closest to EYP, while TPP (EYP modified by TP) had the most different flavor compared to EYP. This was because VE could induce secondary and tertiary structural changes in EYP and exposed more functional groups for binding with volatile flavor compounds such as hexanal, 1-octen-3-ol, and benzaldehyde, thereby improving the overall flavor of EYP. However, due to its larger molecular weight (1099.62 Da), VE exhibited the limited degree of interaction with EYP, thereby enabling it to preserve the overall flavor profile of EYP. On the other hand, TP possessed most active hydroxyl groups, which easily interacted with EYP, forming new complexes that significantly altered its flavor characteristics. Among the five modified powders, VEP had the highest emulsification, but it was still lower than that of EYP. This was because the particle size of VEP (1592.75 nm) was higher than that of EYP (821.88 nm), which was not conducive to the rapid movement to the oil-water interface, resulting in the reduced emulsification.

Preparation of Transglutaminase-Catalyzed Rice Bran Protein Emulsion Gels as a Curcumin Vehicle.

Protein-based emulsion gels have tunable viscoelasticity that can be applied to improve the stability of bioactive ingredients. As the by-product of rice processing, rice bran protein (RBP) has high nutritional value and good digestibility, exhibiting unique value in the development of hypoallergenic formula. In this study, the effect of transglutaminase (TGase) cross-linking on the physicochemical properties of RBP emulsion gels was investigated. To improve the stability of curcumin against environmental stress, the entrapment efficiency and stability of curcumin in the emulsion gel systems were also evaluated. The results indicated that TGase increased the viscoelastic modulus of RBP emulsion gels, resulting in a solid-like structure. Moreover, the entrapment efficiency of curcumin was increased to 93.73% after adding TGase. The thermal stability and photo-stability of curcumin were enhanced to 79.54% and 85.87%, respectively, compared with the sample without TGase addition. The FTIR results showed that TGase induced the cross-linking of protein molecules and the secondary structure change in RBP. Additionally, SEM observation confirmed that the incorporation of TGase promoted the formation of a compact network structure. This study demonstrated the potential of RBP emulsion gels in protecting curcumin and might provide an alternative strategy to stabilize functional ingredients.

Position Matters: Pyridine Regioisomers Influence Secondary Structure and Micelle Morphology in Polymer-Homopolypeptide Micelles.

Polymer-homopolypeptide block copolymers are a class of bioinspired materials that combine the processability and stability of synthetic polymers with the biocompatibility and unique secondary structures of peptides, such as α-helices and β-sheets. These properties make them ideal candidates for a wide variety of applications, for example, in the pharmaceutical field, where they are frequently explored as building blocks for polymeric micelle drug delivery systems. While homopolypeptide side chains can be furnished with an array of different moieties to impart the copolymers with desirable properties, such as stimulus responsivity, pyridine derivatives represent an underutilized functional group for this purpose. Additionally, the interplay between polypeptide side chain structure, secondary conformation, and micelle morphology is not yet well understood, particularly in the case of structural regioisomers. Therefore, in this work, a series of polymer-homopolypeptide copolymers were prepared from a poly(ethylene glycol)-b-poly(glutamic acid) (PEG-b-PGA) backbone, where the pendant carboxylic acid groups were covalently conjugated to a series of pyridine regioisomers by carbodiimide coupling. These pyridine regioisomers differed only in the position of the nitrogen heteroatom, ortho, meta or para, relative to the linking group, generating a series of PEG-b-poly(pyridinylmethyl glutamate) (PEG-b-PMG) copolymers. Following self-assembly of the copolymers in aqueous solutions, dynamic light scattering (DLS) revealed differences in micelle hydrodynamic diameter (Dh) (ranging from ∼60 to 120 nm), while transmission electron microscopy (TEM) and small-angle X-ray scattering (SAXS) revealed distinctive morphologies ranging from ellipsoidal, to cylindrical, and disc-like, suggesting that subtle changes in positional isomers in the polypeptide block may influence the micelle structure. Analysis of the PEG-b-PMG copolymer micelles by circular dichroism (CD) and attenuated total reflectance Fourier transform infrared (ATR-FTIR) spectroscopy revealed that differences in the morphology were associated with changes in polypeptide secondary structure, which in turn was influenced by the position of the pyridine heteroatom. Overall, these findings contribute to the broader understanding of the relationship between polypeptide structure and micelle morphology and serve as useful insight for the rational design of polymer-polypeptide nanoparticles.

Insights into the starch and proteins molecular structure changes of foxtail millet sourdough: Effect of fermentation from grains of cereal to pre-meal

This study investigated the effects of foxtail millet sourdough fermentation time (0, 8, 16, and 24 h) on the protein structural properties, thermomechanical, fermentation, dynamic rheological, starch granules crystalline regions molecular mobility, and starch microstructural characteristics. The fermentation led to a significant increase in the concentration of free amino acids from protein hydrolysis. Fourier transform infrared spectroscopy (FTIR) revealed changes in protein secondary structure and the presence of functional groups of different bioactive compounds. The result of thermomechanical properties showed a significant increase in the stability (0.70–0.79 min) and anti-retrogradation ability (2.29–3.14 Nm) of lactic acid bacteria (LAB) sourdough compared to the control dough, showing a wider processing applicability with radar profiler index. In contrast, sourdoughs with lower tan δ values had higher elasticity and strength. Scanning electron microscopy showed that the surface of the starch appeared from smooth to uneven with patchy shapes and cavities, which declined the crystallinity from 34.00 % to 21.57 %, 23.64 %, 25.09 %, and 26.34 % respectively. Fermentation changed the To, Tp, Tc, and ΔH of the starch. The results of the study will have great potential for application in the whole grain sourdough industry.

Pea protein-inulin conjugate prepared by atmospheric pressure plasma jet combined with glycosylation: structure and emulsifying properties.

Pea protein is one of plant proteins with high nutritional value, but its lower solubility and poor emulsifying properties limit its application in food industry. Based on wet-heating glycosylation of pea protein and inulin, effects of discharge power of atmospheric pressure plasma jet (APPJ) on structure, solubility, and emulsifying ability of pea protein-inulin glycosylation conjugate were explored. Results indicated that the APPJ discharge power did not affect the primary structure of pea protein. However, changes in secondary and spatial structure of pea protein were observed. When APPJ discharge power was 600 W, the solubility of glycosylation conjugate was 75.0% and the emulsifying stability index was 98.9 min, which increased by 14.85 and 21.95% than that of only glycosylation sample, respectively. These findings could provide technical support for APPJ treatment combination with glycosylation to enhance the physicochemical properties of plant-based proteins.

Interaction between ammonium based ionic liquids and CRABP I Protein: A microenvironmental spectroscopic analysis

In this article, we have used circular dichroism (CD) and fluorescence to study the physicochemical behaviour of a β-sheet protein, CRABP I, in the presence of ammonium-based ionic liquids (ILs) as a co-solvent. From fluorescence spectroscopy, a rise in intensity was observed in the presence of ionic liquids in the micromolar range, but a reversal in fluorescence intensity at higher concentrations (millimolar range). The microenvironment of aromatic amino acids, tyrosine (Tyr) and tryptophan (Trp), have been compared using synchronous fluorescence data, and the results demonstrate a similar trend in both cases as it has been seen in steady-state spectra. By using CD spectroscopy to examine conformational behaviour, we found that the protein's secondary structure hardly changes at all. Functionality test showed marginal changes in secondary structure of the protein in the presence of ionic liquids. Binding study revealed the contribution of van der waal’s interaction in the case of N2, N4 and N6 and hydrophobic force in the case of N8. The computational study demonstrated that these biophysical behaviours can be accounted for by the hydrophobic interactions between proteins and ionic liquids.

Using Gaussian accelerated molecular dynamics combined with Markov state models to explore the mechanism of action of new oral inhibitors on Complex I

In this study, our focus was on investigating H-1,2,3-triazole derivative HP661 as a novel and highly efficient oral OXPHOS inhibitor, with its molecular-level inhibitory mechanism not yet fully understood. We selected the ND1, NDUFS2, and NDUFS7 subunits of Mitochondrial Complex I as the receptor proteins and established three systems for comparative analysis: protein-IACS-010759, protein-lead compound 10, and protein-HP661. Through extensive analysis involving 500 ns Gaussian molecular dynamics simulations, we gained insights into these systems. Additionally, we constructed a Markov State Models to examine changes in secondary structures during the motion processes.The research findings suggest that the inhibitor HP661 enhances the extensibility and hydrophilicity of the receptor protein. Furthermore, HP661 induces the unwinding of the α-helical structure in the region of residues 726–730. Notably, key roles were identified for Met37, Phe53, and Pro212 in the binding of various inhibitors. In conclusion, we delved into the potential molecular mechanisms of triazole derivative HP661 in inhibiting Complex I. These research outcomes provide crucial information for a deeper understanding of the mechanisms underlying OXPHOS inhibition, offering valuable theoretical support for drug development and disease treatment design.

In vitro susceptibility of grass carp fish (Ctenopharyngodon idella) to oxidized myosin on structural change of protein secondary structure associated with reactive oxygen species (ROS) treatment

This study aimed to investigate the in vitro susceptibility of grass carp (Ctenopharyngodon idella) oxidized myosin, with the treatment of H2O2 levels being 0, 25, 50, and 100 μmol/L, respectively. The results showed that in vitro oxidation of myosin, reactive oxidative species promoted protein modifications that propagated the conformation changes on myosin secondary structure, leading to a significant increase (P < 0.05) in the protein carbonyl content in the high oxidation treatment, when compared to the low and medium treatments. The results of the Western blot analysis and sodium-polyacrylamide amide-dodecyl sulfate gel electrophoresis demonstrated that in vitro oxidation actively promoted the degradation of protein molecular weight and Desmin (53 kDa) deterioration in the sample with the highest concentration treatment of H2O2. Circular dichroism spectra showed a decrease in α-helix content from 70.1% to 29.8% and an increase in β-sheet percentage from 5.6% to 17.4%. Meanwhile, cysteine and methionine as the free amino acids were most susceptible to oxidative change due to their high sensitivity to the reaction of the sulfur group of amino acids. Protein degradation induced by oxidation resulted in significant changes to the protein secondary structure, as evidenced by the observation of oxidized myosin under different H2O2 levels.

Synergistic coupling of flocculation and fenton reaction for enhanced sludge dewatering: Pivotal role of bi-functional cationic tannin

The challenges associated with sludge dewatering are primarily attributed to the rigid structure formed through the combination of sludge extracellular polymeric substances (EPS) and bound water. Although Fenton oxidation can effectively break down sludge EPS, it faces several challenges including the tough reduction of Fe3+ and the need for large quantities of reagents. In this study, we prepared a cationic tannin (CT) that performed well in flocculation, while also serving as an effective Fe3+ reducing agent due to its phenolic hydroxyl structure. A novel synergistic process coupling CT and the Fenton reaction, integrating flocculation and oxidation, was established for sludge conditioning and dehydration. This system exhibited superior sludge dewatering performance compared to the individual addition of CT or Fenton oxidation under similar conditions. The specific resistance filtration (SRF) of sludge decreased to 22 × 1011m/kg, and the moisture content of the sludge cake decreased to 63.7%. The observed compositional and secondary structural changes in each layer of the sludge’s EPS further confirm the enhanced efficiency of EPS breakdown and bound water release. Following the conditioning process, the sludge filtrate and mud cake met the necessary discharge requirements and could be further treated and utilized as valuable resources in subsequent processes. Additionally, the cost of the system was obviously lower than that of conventional Fenton reaction. This study proposes the use of CT as a bi-functional material, possessing both flocculation and reduction capabilities. By combining CT with the Fenton reaction, we developed an economical and efficient deep sludge dewatering technology.

Elucidating the structural basis of vitamin B12 derivatives as novel potent inhibitors of PTP1B: Insights from inhibitory mechanisms using Gaussian accelerated molecular dynamics (GaMD) and in vitro study

Vitamin B12 is a group of biologically active cobalamin compounds. In this study, we investigated the inhibitory effects of methylcobalamin (MeCbl) and hydroxocobalamin acetate (OHCbl Acetate) on protein tyrosine phosphatase 1B (PTP1B). MeCbl and OHCbl Acetate exhibited an IC50 of approximately 58.390 ± 2.811 μM and 8.998 ± 0.587 μM, respectively. The Ki values of MeCbl and OHCbl Acetate were 25.01 μM and 4.04 μM respectively. To elucidate the inhibition mechanism, we conducted a 500 ns Gaussian accelerated molecular dynamics (GaMD) simulation. Utilizing PCA and tICA, we constructed Markov state models (MSM) to examine secondary structure changes during motion. Our findings revealed that the α-helix at residues 37–42 remained the most stable in the PTP1B-OHCbl Acetate system. Furthermore, upon binding of OHCbl Acetate or MeCbl, the WPD loop of PTP1B moved inward to the active pocket, forming a closed conformation and potentially obstructs substrate entry. Protein-ligand interaction analysis and MM-PBSA showed that OHCbl Acetate exhibited lower binding free energy and engaged in more residue interactions with PTP1B. In summary, our study confirmed the substantial inhibitory activity of OHCbl Acetate against PTP1B, with its inhibitory potency notably surpassing that of MeCbl. We demonstrated potential molecular mechanisms of OHCbl Acetate inhibiting PTP1B.

Raman spectroscopy in the study of amyloid formation and phase separation.

Neurodegenerative diseases, such as Alzheimer's and Parkinson's, share a common pathological feature of amyloid structure accumulation. However, the structure-function relationship between these well-ordered, β-sheet-rich, filamentous protein deposits and disease etiology remains to be defined. Recently, an emerging hypothesis has linked phase separation, a process involved in the formation of protein condensates, to amyloid formation, suggesting that liquid protein droplets serve as loci for amyloid initiation. To elucidate how these processes contribute to disease progression, tools that can directly report on protein secondary structural changes are needed. Here, we review recent studies that have demonstrated Raman spectroscopy as a powerful vibrational technique for interrogating amyloid structures; one that offers sensitivity from the global secondary structural level to specific residues. This probe-free technique is further enhanced via coupling to a microscope, which affords structural data with spatial resolution, known as Raman spectral imaging (RSI). In vitro and in cellulo applications of RSI are discussed, highlighting studies of protein droplet aging, cellular internalization of fibrils, and Raman imaging of intracellular water. Collectively, utilization of the myriad Raman spectroscopic methods will contribute to a deeper understanding of protein conformational dynamics in the complex cellular milieu and offer potential clinical diagnostic capabilities for protein misfolding and aggregation processes in disease states.

Ovalbumin interaction with polystyrene and polyethylene terephthalate microplastics alters its structural properties

Contaminating microplastics can interact with food proteins in the food matrix and during digestion. This study investigated adsorption of chicken egg protein ovalbumin to polystyrene (PS, 110 and 260 μm) and polyethylene terephthalate (PET, 140 μm) MPs in acidic and neutral conditions and alterations in ovalbumin structure. Ovalbumin adsorption affinity depended on MPs size (smaller > larger), type (PS > PET) and pH (pH 3 > pH 7). In bulk solution, MPs does not change ovalbumin secondary structure significantly, but induces loosening (at pH 3) and tightening (at pH 7) of tertiary structure. Formed soft corona exclusively consists of full length non-native ovalbumin, while in hard corona also shorter ovalbumin fragments were found. At pH 7 soft corona ovalbumin has rearranged but still preserved level of ordered secondary structure, resulting in preserved thermostability and proteolytic stability, but decreased ability to form fibrils upon heating. Secondary structure changes in soft corona resemble changes in native ovalbumin induced by heat treatment (80 °C). Ovalbumin is abundantly present in corona around microplastics also in the presence of other egg white proteins. These results imply that microplastics contaminating food may bind and change structure and functional properties of the main egg white protein.

Radiolysis of myoglobin concentrated gels by protons: specific changes in secondary structure and production of carbon monoxide

While particle therapy has been used for decades for cancer treatment, there is still a lack of information on the molecular mechanisms of biomolecules radiolysis by accelerated ions. Here, we examine the effects of accelerated protons on highly concentrated native myoglobin, by means of Fourier transform infrared and UV–Visible spectroscopies. Upon irradiation, the secondary structure of the protein is drastically modified, from mostly alpha helices conformation to mostly beta elements at highest fluence. These changes are accompanied by significant production of carbon monoxide, which was shown to come from heme degradation under irradiation. The radiolytic yields of formation of denatured protein, carbon monoxide, and of heme degradation were determined, and found very close to each other: G+denatured Mb ≈ G+CO ≈ G-heme = 1.6 × 10–8 ± 0.1 × 10–8 mol/J = 0.16 ± 0.01 species/100 eV. The denaturation of the protein to a beta structure and the production of carbon monoxide under ion irradiation are phenomena that may play an important role in the biological effects of ionizing radiation.