Foods
·
2023
·Vol. 12
·期 10
·1931
·
IF 5.2
Dashan Guo,Yuwei Hou,Hongshan Liang,Lingyu Han,Bin Li,Bin Zhou
The distinctive assembly behaviors of lysozyme (Lys) feature prominently in food, materials, biomedicine, and other fields and have intrigued many scholars. Although our previous work suggested that reduced glutathione (GSH) could induce lysozyme to form interfacial films at the air/water interface, the underlying mechanism is still obscure. In the present study, the effects of GSH on the disulfide bond and protein conformation of lysozyme were investigated by fluorescence spectroscopy, circular dichroism spectroscopy, and infrared spectroscopy. The findings demonstrated that GSH was able to break the disulfide bond in lysozyme molecules through the sulfhydryl/disulfide bond exchange reaction, thereby unraveling the lysozyme. The β-sheet structure of lysozyme expanded significantly, while the contents of α-helix and β-turn decreased. Furthermore, the interfacial tension and morphology analysis supported that the unfolded lysozyme tended to arrange macroscopic interfacial films at the air/water interface. It was found that pH and GSH concentrations had an impact on the aforementioned processes, with higher pH or GSH levels having a positive effect. This paper on the exploration of the mechanism of GSH-induced lysozyme interface assembly and the development of lysozyme-based green coatings has better instructive significance.Keywords:reduced glutathione;lysozyme;defolding;self-assembly
研究领域:
食品科学
·
材料科学
·
生物医学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
Soft Matter
·
2014
·Vol. 10
·期 33
·6161-6171
·
IF 4.151
Wenlong Li,Peiyi Wu
Influence of bovine serum albumin on the phase transition behavior of the synthetic ionic liquid tetrabutylphosphonium styrenesulfonate ([P4,4,4,4][SS]) together with the interactions between [P4,4,4,4][SS] and bovine serum albumin (BSA) was investigated by differential scanning calorimetry (DSC), turbidity measurements, FT-IR, in combination with perturbation correlation moving window (PCMW) and two-dimensional correlation spectroscopy (2DCOS). Our results reveal that the addition of BSA would increase the phase transition temperature but weaken the transition behavior of [P4,4,4,4][SS] solution. DSC and turbidity data show us that the transition temperature of a ternary system with 20 wt% BSA added is 3 °C higher than that with 20% (w/v) [P4,4,4,4][SS] solution. Interactions between [P4,4,4,4][SS] and BSA together with the phase transition behavior of [P4,4,4,4][SS] are responsible for the denaturation of BSA upon heating. PCMW determined the obvious distinctions in LCST of different chemical groups manifesting their various response sequences in the phase separation and denaturation upon heating. Finally, 2DCOS was employed to elucidate the sequential order of chemical group motions during heating. It is worth noting that the appearance of the isosbestic point in the CO groups of FTIR spectra indicates the direct transformation of the conformation of α-helix, random coil to β-sheet and β-turn without an intermediate transition state. Additionally, the phase separation process of ionic liquid is able to recover to the original state before heating while the denaturation of BSA is irreversible after a cooling process.
研究领域:
生物物理化学
·
分子生物学
·
药物递送
·
蛋白质工程
·
化学生物学
✓ 已验证
DOI
高影响因子
COLLOIDS AND SURFACES A-PHYSICOCHEMICAL AND ENGINEERING ASPECTS
·
2016
·
IF 2.76
Shanshan Zhang,Xuerui Chen,Shiping Ding,Qunfang Lei,Wenjun Fang
The interactions of human serum albumin (HSA) with four cationic gemini surfactants and four single-chain surfactants have been investigated from the measurements of fluorescence spectroscopy, dynamic lights scattering (DLS), zeta potential, and circular dichroism (CD). The fluorescence results show the binding strength of surfactants to HSA, along with the blue shift under the maximum emission wavelength ( λ max ) which is sensitive to the protein conformations. It has been found that the hydrodynamic diameters of the protein aggregates are enlarged and the electrokinetic potentials of them get positive with increasing the concentration of the surfactants. The conformational transformation of the secondary structures of surfactant–HSA aggregates has been confirmed through the quantitative analysis of the CD spectra. The isothermal titration microcalorimetry (ITC) has been employed to further analyze the binding process of single-chain surfactants to HSA. The comprehensive results obtained from various approaches have shown that both hydrophobic and electrostatic interactions are present in the cationic surfactant–HSA systems. Compared with the corresponding single-chain surfactants, the gemini ones have much stronger binding ability to induce the unfolding of HSA. These investigations on the interactions between HSA and surfactants with the altered chain architecture in different concentration regimes can facilitate the application of surfactant-protein systems in pharmaceutical, biotechnology and related fields.
研究领域:
生物物理化学
·
分子生物学
·
药剂学
·
蛋白质科学
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药物代谢
·
胶体与界面科学
✓ 已验证
DOI
高影响因子
ADVANCED MATERIALS
·
2025
·
IF 26.8
Ruifen Yang,Ruilin Shang,Jiayan Hu,Zongrui Tong,Lisha Yu,Zhengwei Mao
Marine protein adhesives present robust wet adhesion by mediating interfacial interactions through surface-exposed hydrophobic domains/adhesive groups and maintaining cohesive networks via intrinsically disordered protein structures. Replicating these capabilities in common protein systems remains challenging, especially in stabilizing hydrophobic residues at interface and improving cohesive properties. Here, we developed unfolded protein-based adhesives via a universal strategy of locking with polyelectrolytes that have flexible long chains and high charge density. These polyelectrolytes simultaneously stabilize exposed hydrophobic residues on the unfolded proteins and reinforce cohesion properties via chain entanglement with electrostatic/hydrogen bonding interactions. The unfolded bovine serum albumin (UBSA) and polyacrylic acid (PAA) are integrated to prepare a representative tissue adhesive (UBSA-PAA), exemplifying the polyelectrolyte-locking strategy. The UBSA-PAA adhesive demonstrated interfacial hydrophobicity (water contact angles >90°) and excellent adhesion performance on wet tissue. In severe liver and femoral artery hemorrhage models, this adhesive significantly reduced blood loss compared to commercial fibrin glue, while maintaining comparable biocompatibility. This polyelectrolyte-locking molecular engineering strategy provides a universal framework for designing protein-based adhesives with excellent wet adhesion performance.
研究领域:
材料科学
·
生物医学工程
·
粘合技术
·
分子工程
·
蛋白质化学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
危险品化学品经营许可证（带存储）