Journal of Natural Fibers
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2022
·
IF 3.507
Yun Wang,Xin Liu,Liangjun Xia,Chunhua Zhang,Weilin Xu
Silk fibers were produced by feeding Bombyx mori silkworm larvae with a modified feed of mulberry leaves containing nano Fe3O4 particles. The silkworms were weighed to determine the effect of nano Fe3O4 particles on the growth of larvae. The effects of nano Fe3O4 contents on the morphologies, chemical structures, mechanical properties, and thermal properties of silk were also investigated, respectively. The results indicate that the nano Fe3O4 particles was embedded in the silk. Additionally, the stress and toughness of modified silk were enhanced, as compared with the normal silk. Finally, the integration of the amide I band intensities suggests a relatively high content of β-sheet in the modified silk.
研究领域:
生物学
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材料科学
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DOI
高影响因子
ACS Applied Materials & Interfaces
·
2017
·
IF 7.504
Dihan Su,Meng Yao,Jie Liu,Yiming Zhong,Xin Chen,Zhengzhong Shao
Usually, regenerated silk fibroin (RSF) hydrogels cross-linked by chemical agents such as horseradish peroxide (HRP)/H2O2 perform elastic properties, while display unsatisfactory strength for practical applications especially as load-bearing materials, and inadequate stability when incubated in a simulated in vivo environment. Here, the RSF hydrogel with both excellent strength and elasticity was prepared by inducing the conformation transition from random coil to β-sheet in a restricted RSF network precross-linked by HRP/H2O2. Such “dual-networked” hydrogels, regarding the one with 10 wt % RSF (Mw: 220 kDa) as a representative, show around 100% elongation, as well as the compressive modulus and tensile modulus up to 3.0 and 2.5 MPa respectively, which are much higher than those of physically cross-linked natural polymer hydrogels (commonly within 0.01–0.1 MPa at the similar solid content). It has been shown that the enhanced comprehensive mechanical properties of RSF hydrogels derive from the formation of small-sized and uniformly distributed β-sheet domains in the hydrogel during the conformation transition of RSF whose size is limited by the first network formed by cross-linkers with HRP/H2O2. Importantly, the tough RSF hydrogel changes the normally weak recognition of various RSF hydrogels and holds a great potential to be the material in biomedical field because it seems to be very promising regarding its biocompatibility, biodegradability, etc.
研究领域:
生物材料学
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高分子化学
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生物医学工程
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DOI
PubMed
高影响因子
FOOD CHEMISTRY
·
2025
·
IF 9.8
Min Huang,Li Li,Xinran Cheng,Ran Qiu,Yi Wang,Xianjiang Zhou,Xuyan Zong
Some starch in distiller's grains has low utilization rate and serious waste of resources due to its combination with endogenous non-starch components (proteins). This study explored the impact of removing different endogenous proteins on starch molecules' physicochemical structure and brewing characteristics. Results revealed β-sheet-dominated proteins in fermented grains, with alkali-soluble proteins being most abundant (37.47 %). The removal of protein resulted in the formation of a porous structure on the surface of starch. The swelling degree, freeze-thaw stability and in vitro digestion characteristics of each sample were significantly improved except as solubility. Among them, alcohol-soluble protein had obvious promoting effect on pore formation and gelatinization, and both alcohol-soluble protein and alkali-soluble protein could weaken the interaction of starch complex and improve the brewing performance. This provides a new idea for improving the efficient utilization of starch and reducing the waste of resources in the future liquor brewing process.
研究领域:
食品科学
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生物化学
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产品关联
DOI
PubMed
高影响因子
FOOD CHEMISTRY
·
2024
·
IF 8.5
Xiaohan Zheng,Bowen Zou,Ruitao Zhu,Junwei Zhang,Xiaokang Na,Ming Du,Beiwei Zhu,Chao Wu
Structured binary protein networks offer a pathway for designing gel-based foods with less ecological and economic effects. This study investigated the heat-mediated interaction and gelation kinetics of cod-soy mixed proteins at molecular level. Results indicated that denaturation degree of soy proteins was fundamental in determining the protein-protein interactions during heating. Considerable non-natural β-sheet was generated in the heterogeneous structures to initiate their aggregation behavior. Cod actomyosin comprising myosin heavy chains and actin mainly regulated their aggregation below 70 °C. At higher temperatures, the formation of large-sized and intermediary-sized aggregates was dominated by disulfide bond exchange between cod actomyosin and soy A-B aggregates (≤ 85 °C) or dissociated B subunits (> 85 °C). These aggregates were further evidenced as essential components to form gel networks with higher storage modulus (G'). These findings provide fundamental insights for designing gel-based products with desirable nutritional and textural properties based on plant-animal binary proteins.
研究领域:
食品科学
·
分子生物学
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DOI
PubMed
高影响因子
BIOMACROMOLECULES
·
2018
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IF 5.738
Yuchen Guo,Sha Wang,Hanhan Du,Xiaolong Chen,Hao Fei
Understanding the chemical absorption process of silver ions helps the rational design of functional materials for effective release to minimize unwanted toxicity. To this end, a histidine-containing aliphatic peptide (IH6) was designed to immobilize the silver ion (Ag+) through coordinate interaction. Using circular dichroism spectroscopy, Ag+ was found to dose-dependently induce parallel β-sheet conformation of IH6 to a saturation molar ratio of 1:2. A conformational switch of IH6 from antiparallel to parallel β-sheet assembly upon Ag + coordination was further revealed by Fourier transform infrared spectroscopy. The resultant Ag-IH6 hydrogel displayed substantially enhanced mechanical strength as well as controlled release of Ag+. Ag-IH6 hydrogel thus exhibited strong dose-dependent bactericidal activities that can be tuned selectively, sparing the cocultured human keratinocytes in normal. Overall, the study demonstrates an unusual silver ion-induced peptide conformational switch between β-structure subtypes and the bilateral effects on hydrogel-based chemical control of silver ion absorption and release, thus, revealing the potential in antibacterial applications.
研究领域:
生物化学
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材料科学
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微生物学
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DOI
PubMed
高影响因子
POLYMER JOURNAL
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2020
·Vol. 52
·期 12
·1395-1400
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IF 2.826
Wu Jianbing,Guo Wenjun,Zhang Lixiang,Wang Yongfeng,Liu Leigen,Wang Wei,Sun Yinyin,Tao Jin,Wang Xiaoqin
The present study described a new method with one step to fabricate silk fibroin nano- and microspheres, with the size of spheres and crystalline structure being controllable during processing. Polyethylene glycol, a type of synthetic polymer that is widely used in the pharmaceutical industry as a formulation excipient, was utilized to induce silk fibroin to self-assemble into nano- and microspheres. The addition of a certain amount of salt in the blending solution with subsequent titration into ethanol could improve the size dispersion, yield, and crystalline β-sheet structure (silk II) compared to those prepared without salt addition during preparation. Silk microspheres prepared in the presence of salts were less porous and more homogeneous in size than those prepared in the absence of salts.
研究领域:
材料科学
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生物医学工程
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产品关联
DOI
高影响因子
Materials Science & Engineering C-Materials for Biological Applications
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2017
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IF 4.164
Jianbing Wu,Xusheng Xie,Zhaozhu Zheng,Gang Li,Xiaoqin Wang,Yansong Wang
The effects of changing solution pH in the range of 3.6–10.0 during a one-step silk microsphere preparation process, by mixing silk and polyethylene glycol (PEG), was assessed. The microspheres prepared at low pH (3.6) showed a more homogeneous size (1–3 μm) and less porous texture than those prepared at neutral pH. High pH (10.0) inhibited microsphere formation, yielding small and inhomogeneous microspheres. Compared to neutral pH, low pH also increased the content of silk crystalline β-sheet structure from approx. 30% to above 40%. As a result, the microspheres produced at low pH were more thermally stable as well as resistant to chemical (8 M urea) and enzymatic (protease XIV) degradation when compared to microspheres prepared at neutral pH. Doxorubicin hydrochloride (DOX) and curcumin (CUR) were successfully loaded in silk microspheres via control of solution pH. The loading efficiency of DOX was approx. 95% at pH 7.0 and approx. 60% for CUR at pH 3.6, attributed to charge-charge interactions and hydrophobic interactions between the silk and drug molecules, respectively. When PBS, pH 7.4, was used as a medium for release studies, the pH 3.6 microspheres released both drugs more slowly than the pH 7.0 microspheres, likely due to the high content of crystalline β-sheet structure that enhanced drug-silk interactions as well as restricted drug molecule diffusion.
研究领域:
生物材料
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药剂学
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DOI
PubMed
高影响因子
Polymer Chemistry
·
2013
·Vol. 4
·期 21
·5425-5431
·
IF 5.231
Li Ma,Yuhong Yang,Jinrong Yao,Zhengzhong Shao,Xin Chen
Soy protein based materials are of great interest because of the merits of biocompatibility, biodegradability, renewability, etc. However, the poor mechanical properties and high water sensitivity limit their further application in many fields. In this paper, we tried to overcome these shortcomings through a slight chemical modification of the polypeptide chains of soy protein. 31P NMR and solid state 13C CP/MAS NMR spectroscopy confirmed that the diethoxy phosphoryl groups were successfully grafted onto soy protein chains with a molar grafting ratio of 0.15–1.18%, which almost did not change the nature of soy protein. The isoelectric point and rheological behavior of the modified soy protein sample varied with the grafting ratio, indicating that the tertiary structure of the protein was changed after phosphoryl modification. The FTIR spectra of the modified soy protein suggested that the increase of β-sheet conformation from the slight chemical modification could be the reason for the change of the globular structure of soy protein. Finally, we obtained a robust soy protein film as expected, and we did not use any crosslinking agent and plasticizer that were almost unavoidable in the previous studies reported in the literature. The tensile strength and the elongation at break of our soy protein films were 35 ± 5 MPa, 2.5 ± 0.5% in the dry state, and 3.8 ± 1.5 MPa, 125 ± 5% in the wet state, respectively. We believe that the method we developed in this communication provides a practical approach to improve the mechanical properties and broaden the applications of natural soy protein based materials.
研究领域:
材料科学
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食品科学
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生物化学
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产品关联
DOI
高影响因子
ACS Nano
·
2023
·
IF 17.1
Shuo Yang,Chenxi Zhao,Yunhao Yang,Jing Ren,Shengjie Ling
Animal silk is usually considered to exist as a solid fiber with a highly ordered structure, formed by the hierarchical assembly starting from a single silk fibroin (SF) chain. However, this study showed that silk protein molecules existed in the form of a fractal network structure in aqueous solution, rather than as a single chain. This type of network was relatively rigid with low fractal dimension. Finite element analysis revealed that this network structure significantly helped in the stable storage of SF prior to the spinning process and in the rapid formation of a β-sheeted nanocrystalline and nematic texture during spinning. Further, the strong but brittle mechanical properties of Bombyx mori silk could also be well-explained through the fractal network model of silk fibroin. The strength was mainly derived from the dual network structure, consisting of nodes and β-sheet cross-links, whereas the brittleness could be attributed to the rigidity of the SF chains between these nodes and cross-links. In summary, this study presents insights from network topology for understanding the spinning process of natural silk and the structure–property relationship in silk materials.
研究领域:
生物材料学
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分子生物学
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材料科学
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产品关联
DOI
PubMed
高影响因子
FOOD HYDROCOLLOIDS
·
2019
·
IF 5.839
Zhibiao Feng,Lele Li,Yu Zhang,Xuan Li,Chunhong Liu,Bin Jiang,Jing Xu,Zhigang Sun
Nanofibrils have favorable functional properties that facilitate their applications in the food industry. Whey protein isolate (WPI) is widely used to prepare nanofibrils via acid hydrolysis. In this research, the effect of hydrolysis by endoproteinase GluC (GluC) on WPI nanofibrils (WPNFs) was evaluated based on their structural and emulsifying properties. Following the hydrolysis of WPI by GluC at 37 °C and pH 8.0, the peptides self-assembled into WPNFs at 37 °C and pH 2.0. WPNFs with several micrometric length and nanometric (1–10 nm) diameter exhibited high aspect ratio (length/diameter). Based on microscopic images, circular dichroism spectroscopy , and infrared spectroscopy , we concluded that β-sheets played an important role in the formation and stability of WPNFs. The main factor affecting WPNF formation was found to be hydrolysis by GluC for 10 h followed by aggregation at pH 2.0. Whey protein hydrolysates with glutamic acid or aspartic acid residues, obtained from WPI hydrolysis by GluC for 10 h, might be positively charged in an acidic environment, thereby favoring the formation of ordered aggregates instead of random ones. WPNFs prepared under such conditions have a strong ability of improving the oxidative stability, activity and stability of emulsions . This new strategy for producing WPNFs will potentially expand their application in the food industry.
研究领域:
食品科学
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生物化学
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DOI
高影响因子
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2024
·
IF 7.7
Xiaohan Zheng,Bowen Zou,Wenqiang Cai,Xianbing Xu,Ming Du,Xiaokang Na,Beiwei Zhu,Chao Wu
Cod proteins (CPs) have potential applications in designing desirable gel-based products, and this study aimed to unravel their heat-induced aggregation pattern and further probe the roles in protein gels. SDS-PAGE analysis indicated that high-precipitation-coefficient aggregates (HPCAs) of CPs aggregates were composed of considerable polymers of myosin heavy chains and actin, and their low-precipitation-coefficient aggregates (LPCAs) contained myosin light chains and tropomyosin . Studies from correlation analysis between the structure and aggregation kinetics revealed that the generation of β-sheet and S S bonds were responsible for their spontaneous thermal aggregation induced by heating temperature and protein concentration, respectively. Additionally, as protein denaturation ratio increased, more and larger HPCAs were formed, which was evidenced driving the network formation of protein gels and resulting in higher storage modulus (G') values. These novel findings may be applicable to other animal proteins for better tailoring the manufacturing of muscle gel-based products.
研究领域:
食品科学
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生物化学
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DOI
PubMed
高影响因子
CHEMISTRY-A EUROPEAN JOURNAL
·
2016
·Vol. 22
·期 44
·15751-15759
·
IF 5.771
Jingfang Li,Xiaodong Li,Jing Xu,Yang Wang,Lixin Wu,Yanqiu Wang,Liyan Wang,Myongsoo Lee,Wen Li
Graphical Engineered assembly : The self-assembly behavior of polyoxometalates and cationic peptides is dependent on the competitive interactions, including hydrogen-bonds, hydrophobic, π-π interactions, electrostatic repulsion, and the steric hindrance. These driving forces can be regulated by the subtle alterations of the size of polyoxometalates and/or the residues of peptides, resulting in controllable nanostructures (see scheme). The self-assembly behavior of polyoxometalates (PMs) and facial-like cationic peptides carrying lysine residues were systematically investigated. Circular dichroism and UV/Vis spectra demonstrated that the multivalent electrostatic attractions between polyanionic PMs and short peptides with protonated lysine residues initiated the conformational transition of peptide molecules from random-coil to β-sheet state, and subsequently the co-assembly. TEM and atomic force microscopy (AFM) measurements showed that uniform nanofibers formed with decreasing size of the PMs or increasing the intermolecular forces of the peptides, such as through hydrogen-bonding, hydrophobic, and/or π–π interactions. Additionally, the stability of the nanostructures can be improved by rational suppression of the electrostatic repulsion of the shell peptides covering the surface of the nanostructures. These results provide new insight into understanding the ionic self-assembly of peptides and PMs and controlling their final morphology.
研究领域:
材料科学
·
生物化学
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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）