摘要：
In this study, bovine collagen peptide (BCP) decorated selenium nanoparticles (BCP-SeNPs) were prepared using BCP as a protective and reducing agent, and their structure, hypolipidemic and antitumor activities were investigated. The results of the various techniques including dynamic light scattering (DLS), transmission electron microscopy (TEM), energy dispersive x-ray (EDX) spectroscopy, x-ray photoelectron spectroscopy (XPS), circular dichroism (CD) spectroscopy, Fourier transform infrared (FT-IR) spectroscopy confirmed the successful synthesis of BCP-SeNP. The polydispersity index (PDI) and zeta-potential analysis displayed that the PDI of BCP-SeNPs was about 0.12, smaller than BCP. The zeta-potential absolute value of BCP-SeNPs was found to be 34.2 mV, higher than BCP, suggesting that the stability of the BCP-SeNPs was better than BCP. Hypolipidemic performance evaluation indicated that binding capacity of BCP-SeNPs to bile salts was the highest when its concentration was 0.3 mM, and significantly higher than bare SeNPs, bovine serum albumin decorated SeNPs (BSA-SeNPs), and hyaluronic acid decorated SeNPs (HA-SeNPs). Moreover, the viability of HepG2 cells after BCP-SeNPs treatment was only 22.95%, which was considerably lower than that of bare SeNPs, BSA-SeNPs, and HA-SeNPs, showing better antitumor activity. These findings are expected to provide novel active ingredients that can be employed as functional foods and drugs.
通讯机构：
[Wei, BM ] W;[Wang, HB ] H;Wuhan Polytech Univ, Sch Chem & Environm Engn, Wuhan, Hubei, Peoples R China.;Hubei Engn Univ, Coll Life Sci & Technol, Hubei Key Lab Qual Control Characterist Fruits & V, Xiaogan, Hubei, Peoples R China.
摘要：
A significant focus of carbon dot research is on enhancing the fluorescence emission performance of biomimetic carbon dots to improve their application value in practical analysis. In this study, fish scales were used as a precursor, and citric acid was introduced to improve the quantum yield of carbon dots. The results showed that under 350 nm excitation, citric acid-modified carbon dots (CDs-FS/CA) exhibited a maximum fluorescence emission of 411 nm, and the emission behavior was independent of the excitation wavelength, with a quantum yield of 35.5%. This high quantum yield could be attributed to the presence of citric acid and the participation of hydroxyapatite in fish scales. The CDs-FS/CA had a moderate degree of graphitization, smaller and more concentrated particle size distribution, and a high proportion of pyrrole N. They showed good fluorescence performance through the synergistic effect of surface state sp2 C and different N-doped surface states. A good linear relationship in the range of 0-50 mu mol L-1 was obtained using CDs-FS/CA for trace detection of quercetin, with a limit of detection of 3.8 nmol L-1, and good recovery in actual sample detection. These results offer a reference for enhancing the quantum yield of CDs obtained from alternative biomass sources and indicate the encouraging commercial feasibility of CDs derived from waste biomass for detecting trace amounts of quercetin. Through modification, this work significantly enhances the quantum yield of carbon dots derived from fish scales and applies them for trace detection of quercetin.
摘要：
Mineral elements including calcium, iron, and zinc play crucial roles in human health. Their deficiency causes public health risk globally. Commercial mineral supplements have limitations; therefore, alternatives with better solubility, bioavailability, and safety are needed. Chelates of food-derived peptides and mineral elements exhibit advantages in terms of stability, absorption rate, and safety. However, low binding efficiency limits their application. Extensive studies have focused on understanding and enhancing the chelating activity of food-derived peptides with mineral elements. This includes obtaining peptides with high chelating activity, elucidating interaction mechanisms, optimizing chelation conditions, and developing techniques to enhance the chelating activity. This review provides a comprehensive theoretical basis for the development and utilization of food-derived peptide-mineral element chelates in the food industry. Efforts to address the challenge of low binding rates between peptides and mineral elements have yielded promising results. Optimization of peptide sources, enzymatic hydrolysis processes, and purification schemes have helped in obtaining peptides with high chelating activity. The understanding of interaction mechanisms has been enhanced through advanced separation techniques and molecular simulation calculations. Optimizing chelation process conditions, including pH and temperature, can help in achieving high binding rates. Methods including phosphorylation modification and ultrasonic treatment can enhance the chelating activity.
摘要：
Food-derived peptides (FPs) are bioactive molecules produced from dietary proteins through enzymatic hydrolysis or fermentation. These peptides exhibit various biological activities. However, their efficacy largely depends on bioavailability, the ability to cross absorption barriers, and reach target sites within the body. This review addresses key issues in FP absorption, including barriers, pathways, influencing factors, and strategies to enhance absorption. The biochemical and physical barriers to FP absorption include pH variations, enzymes, unstirred water layer, mucus layer, and intestinal epithelial cells. FPs enter the bloodstream via four main pathways: carrier-mediated transport, endocytosis, paracellular, and passive diffusion. The barrier-crossing efficiency depends on the structural properties and state of FPs and coexisting substances. Absorption efficiency can be significantly improved with permeability enhancers, nano-delivery systems, and chemical modifications. These insights provide a scientific basis and practical guidance for optimizing the bioactivity and health benefits of food-derived peptides.
Food-derived peptides (FPs) are bioactive molecules produced from dietary proteins through enzymatic hydrolysis or fermentation. These peptides exhibit various biological activities. However, their efficacy largely depends on bioavailability, the ability to cross absorption barriers, and reach target sites within the body. This review addresses key issues in FP absorption, including barriers, pathways, influencing factors, and strategies to enhance absorption. The biochemical and physical barriers to FP absorption include pH variations, enzymes, unstirred water layer, mucus layer, and intestinal epithelial cells. FPs enter the bloodstream via four main pathways: carrier-mediated transport, endocytosis, paracellular, and passive diffusion. The barrier-crossing efficiency depends on the structural properties and state of FPs and coexisting substances. Absorption efficiency can be significantly improved with permeability enhancers, nano-delivery systems, and chemical modifications. These insights provide a scientific basis and practical guidance for optimizing the bioactivity and health benefits of food-derived peptides.
通讯机构：
[Wang, HB ] H;Hubei Engn Univ, Coll Life Sci & Technol, Hubei Key Lab Qual Control Characterist Fruits & V, Xiaogan, Hubei, Peoples R China.
关键词：
Fish scale collagen hydrolysate;Plastein reaction;Antioxidant properties;Reactive oxygen species
摘要：
An important area of focus for developing antioxidant collagen hydrolysates (peptides) involves enhancing the antioxidant properties of collagen hydrolysates. In this study, fish scale collagen hydrolysate (FH) was used as the raw material for plastein reaction. Various enzymes, including papain, alcalase, flavourzyme, and the combination of alcalase and flavourzyme, were employed for this purpose. The plastein reaction significantly improved the thermal stability, chemical antioxidant activity, and capacity to scavenge cellular reactive oxygen species of FH. Notably, the plastein reaction catalyzed by alcalase exhibited the most significant improvement, increasing the hydroxyl radical scavenging rate from 72.3 to 93.4% and restoring the viability of the oxidative stress-induced HepG2 cell model from 50.8 +/- 1.7 to 74.9 +/- 1.7%. During the plastein reaction, condensation and hydrolysis reactions occurred simultaneously, with condensation being the dominant process. These reactions, along with physical aggregation, facilitated the formation of larger yet more concentrated collagen peptide aggregates, leading to increased exposure of hydrophobic groups. This enhanced the uptake of collagen hydrolysates by the cells and contributed to the enhancement of their antioxidant properties. Thus, the plastein reaction is an effective method for enhancing the antioxidant properties of collagen hydrolysates, with its simplicity of operation and promising application potential.
期刊：
Collagen and Leather,2024年6(1):1-11 ISSN：2097-1419
通讯作者：
Haibo Wang
作者机构：
[Evgeny A. Shirshin] Department of Physics, M. V. Lomonosov Moscow State University, Leninskie Gory 1/2, 119991, Moscow, Russia;[Tianyi Liu] School of Food Science and Engineering, Wuhan Polytechnic University, Wuhan, Hubei, China;[Chengzhi Xu; Benmei Wei; Haofei Xu; Peishan Sui; Yang Liu; Juntao Zhang] School of Chemical and Environmental Engineering, Wuhan Polytechnic University, Wuhan, Hubei, China;Oil Crops Research Institute, Chinese Academy of Agricultural Sciences, Key Laboratory of Oilseeds Processing, Ministry of Agriculture, Hubei Key Laboratory of Lipid Chemistry and Nutrition, Wuhan, Hubei, China;[Haibo Wang] College of Life Science and Technology, Hubei Key Laboratory of Quality Control of Characteristic Fruits and Vegetables, Hubei Engineering University, Xiaogan, Hubei, China
通讯机构：
[Haibo Wang] C;College of Life Science and Technology, Hubei Key Laboratory of Quality Control of Characteristic Fruits and Vegetables, Hubei Engineering University, Xiaogan, China
摘要：
<div class="mag_zhaiyao_sec"><p id="Par1" class="mag_zhaiyao_p">The limitations of native collagen, such as thermal stability and solubility in physiological environments, can be improved by applying bioconjugation and synthetic chemistry techniques. However, the exquisite control of the modification site of collagen remains a challenge. In this work, pH-responsive poly(acrylic acid) (PAA) with different chain lengths was attached to the N-terminal α-amino groups of succinylated collagen using a site-specific modification strategy. Additionally, the structure, thermal stability, and pH sensitivity of succinylated collagen were explored. The modification rate of amino groups in the succinylated collagen-PAA bioconjugate (SPSC-PAA) was evaluated by the 2,4,6-trinitrobenzene sulfonic acid assay. The impact of N-terminal modification of PAA and its chain length on the thermal stability of collagen was explored by CD and DSC. These techniques revealed that the thermal stability of SPSC-Col is pH-responsive and closely related to the chain length of grafted PAA. The pH sensitivity of SPSC-PAA was further explored by rheology and turbidity. Subsquently, the critical pH and isoelectric point of SPSC-PAAs were also examined by turbidity and isoelectric point titration, respectively. This work provides a new insight into the N-terminal modification of collagen on its properties.</div> <div id="ASec2" class="mag_zhaiyao_sec"><strong class="mag_zhaiyao_title">Graphical abstract </strong></div>
摘要：
Customized control of the biological response between the material matrix and cells is a crucial aspect in the development of the next generation of collagen materials. This study aims to investigate the effects of ultrahigh pressure treatment on the interaction between collagen and cells by subjecting bovine tendon collagen to different intensities of ultrahigh pressure field. The results indicate that ultrahigh pressure treatment alters the spatial folding of collagen, causing distortion of its triple helical conformation and exposing more free amino groups and hydrophobic regions. As a result, collagen's cell adhesion capability and ability to promote cell migration are significantly enhanced. Optimal cell adhesion and migration capabilities are observed in collagen samples treated at 500 MPa for 15 min. However, further increasing the intensity of the ultrahigh pressure treatment leads to severe damage to the triple-helical structure of collagen, along with re-aggregation of free amino groups and hydrophobic moieties, thereby reducing collagen's cell adhesion capability and ability to promote cell migration. Therefore, ultrahigh pressure treatment offers a promising method to effectively regulate collagen-cell adhesion and promote cell migration without the need for external components. This provides a potential means for the customized enhancement of collagen-based material interfaces .
Customized control of the biological response between the material matrix and cells is a crucial aspect in the development of the next generation of collagen materials. This study aims to investigate the effects of ultrahigh pressure treatment on the interaction between collagen and cells by subjecting bovine tendon collagen to different intensities of ultrahigh pressure field. The results indicate that ultrahigh pressure treatment alters the spatial folding of collagen, causing distortion of its triple helical conformation and exposing more free amino groups and hydrophobic regions. As a result, collagen's cell adhesion capability and ability to promote cell migration are significantly enhanced. Optimal cell adhesion and migration capabilities are observed in collagen samples treated at 500 MPa for 15 min. However, further increasing the intensity of the ultrahigh pressure treatment leads to severe damage to the triple-helical structure of collagen, along with re-aggregation of free amino groups and hydrophobic moieties, thereby reducing collagen's cell adhesion capability and ability to promote cell migration. Therefore, ultrahigh pressure treatment offers a promising method to effectively regulate collagen-cell adhesion and promote cell migration without the need for external components. This provides a potential means for the customized enhancement of collagen-based material interfaces .
摘要：
Collagen self-assembly into fibrous structures is a phenomenon that attracts wide attention in the biomedical and tissue engineering material fields. However, collagen's shortcoming of low thermal stability limits its application. Trehalose, a well-known compatible osmolyte, can stabilize proteins against various denaturing conditions. Herein, the effect of trehalose on the self-assembly and conformational stability of collagen was explored. The effect of trehalose on self-assembly was studied with turbidity, chloramine T assay, rheology, SEM and TEM characterizations. Circular dichroism (CD) was used to monitor the impact of trehalose on the triple helical conformation stability of collagen. The obtained experimental results reveal that trehalose could (1) accelerate the self-assembly kinetics and improve the self-assembly degree of collagen and the mechanical properties of the resulting hydrogels, but has no impact on the microstructure of the resulting collagen fibrils, and (2) increase the thermal stability of collagen. Both are desirable for the industrial application of collagen-based materials. Furthermore, the MTT assay and cell morphology characterization suggest that trehalose has no effect on the cytocompatibility of collagen materials.
摘要：
As a major component of extracellular matrixes (ECMs), collagen is an attractive biomaterial to fabricate porous scaffold for tissue engineering due to their similarity to the in vivo static microenvironment. However, the collagen-based porous scaffolds were difficult to mimic the dynamically remolded porous structure of ECM during the cell proliferation and tissue development, and always have poor mechanical property and not easy to handle. Here, natural collagen and partially denatured collagen was used to prepare the stepwise degradable hybrid bioscaffold with suitable mechanical property and dynamically remolded inner porous structure, which is desirable for the applications of tissue engineering. The collagen-based microporous scaffold was first prepared and used as physical support, then, the mechanical strength of which was reinforced by the import of the partially denatured collagen to give the hybrid bioscaffold. The fabrication conditions of the hybrid scaffolds were optimized, of which the thermal stability, mechanical property, and swelling property was explored. The stepwise enzymatic degradation process and the corresponding porous structure variation of the hybrid scaffold was confirmed by SEM and cell culture assays.
通讯机构：
[Chengzhi Xu; Haibo Wang] S;School of Chemistry and Environmental Engineering, Wuhan Polytechnic University, Wuhan, Hubei, P. R. China<&wdkj&>School of Chemistry and Environmental Engineering, Wuhan Polytechnic University, Wuhan, Hubei, P. R. China
摘要：
Collagen-polymer conjugates are being developed rapidly based on advancements in both polymer and protein science. The attachment of polymers to proteins can be achieved with the "grafting to" method or the "grafting from" method; the latter is more attractive. Although polymer-based collagen engineering provides an attractive strategy to regulate the native functions of collagen, there are still two important unresolved issues: the harsh modification conditions and the loss of fibrillogenesis property. Herein, a collagen-PNIPAAm conjugate (PCol) was prepared by the "grafting from" method to avoid harsh conditions. The amino groups of collagen were modified by a water-soluble NHS-functionalized ATRP initiator before in situ polymerization of NIPAAm on the collagen surface. On the other hand, the fibrillogenesis of PCol was realized by the induction of natural collagen, inspired by the xenogeneic collagen hybrid fibrils in organisms. Furthermore, the structure, fibrillogenesis, thermosensitivity, and biocompatibility of PCol were explored. This work may be useful in synthesizing optimized formulate collagen-polymer conjugates and helpful for the design of the novel collagen-based hybrid materials.
