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Nanofibrous polypeptide hydrogels with collagen-like structure as biomimetic extracellular matrix

collagen and Leather 2023年第2期5卷 81-93页

作者： Chengkun Zhao Xing Li Shaoquan Bian Weinan Zeng Alfredo Ronca Ugo D'Amora Maria Grazia Raucci Jie Liang Yong Sun Qing Jiang Yujiang Fan Luigi Ambrosio Xingdong Zhang National Engineering Research Center for Biomaterials Sichuan University29#Wangjiang RoadChengdu 610064People's Republic of China College of Biomedical Engineering Sichuan University29#Wangjiang RoadChengdu 610064People's Republic of China Shenzhen Institutes of Advanced Technology Chinese Academy of SciencesShenzhen 518055People's Republic of China Orthopedic Research Institution Department of OrthopedicsWest China HospitalSichuan UniversityChengdu 610041People's Republic of China Institute of Polymers Composites and BiomaterialsNational Research Council80125 NaplesItaly

Supramolecular peptides exhibit obvious similarities with collagen fibers in terms of self-assembly characteristics,nanofibrous structure,and responsiveness to external ***,a series of supramolecular peptides were developed by altering the amino acid sequence,enabling the self-assembly of three types of 4-biphenylacetic acid(BPAA)-tripeptides into fibrous hydrogel through hydrogen bonding and n-n stacking under the influence of ion *** electron and scanning electron microscopies revealed that the diameter of the fiber within nanofibrous hydrogels was~10 and~40 nm,respectively,which was similar with the self-assembled collagen *** this reason,these hydrogels could be considered as a biomimetic extracellular ***,the gelation concentration induced by ions was even lower than 0.66 wt%,with an elastic modulus of~0.27 kPa,corresponding to a water content of 99.34 wt%.In addition,the three supramolecular hydrogels were found to be good substrates for L929 cell adhesion and MC-3T3 cell *** overall results implied that BPAA-based hydrogels have a lucrative application potential as cell carriers.

关键词： collagen-like Supramolecular peptides Nanofibrous hydrogel Ion-induction Biomimetic extracellular matrix

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Structural, thermal and enzymatic analysis of naturally occurring and D-amino acid substituted peptides

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Advances in Bioscience and Biotechnology 2012年第7期3卷 900-908页

作者： Velmurugan Punitha Raghava Rao Jonnalagadda Balachandran Unni Nair Council of Scientific and Industrial Research-Central Leather Research Institute Chemical Laboratory Chennai India

Designing of new peptide materials for biomedical and protein engineering applications are important. In the present work an attempt has been made to study the effect of D-Leu in collagen like tetra peptide on the structure and stability of peptide against enzymes and results are compared with its chiral counterpart L-form. Effect of replacement of L-Leu in Leu-Gly-Pro-Ala tetra peptide with D-Leu on structure has been studied using circular dichroic spectroscopy (CD). Our findings suggest that, D-Leu substitution leads to conformational changes in Leu-Gly-Pro-Ala secondary structure from β-sheet to turns. L → D-Leu Configurational changes in Leu-Gly-Pro-Ala owes to enhanced thermal stability which has been substantiated through CD and differential scanning calorimetry. Change in chirality of the leucine inhibits collagenolytic activity, which enables to design selective inhibition of proteases with greater specificity.

关键词： collagen-like Peptide Configurational Change Leu-Gly-Pro-Ala collagen Chirality Amino Acid

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