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基于 SAA/弹性蛋白模拟肽自组装的水凝胶揭示了非经典的纳米拓扑结构。

Hydrogels from the Assembly of SAA/Elastin-Inspired Peptides Reveal Non-Canonical Nanotopologies.

机构信息

Laboratory of Bioinspired Materials (LABIM), Department of Science, University of Basilicata, 85100 Potenza, Italy.

Department of Materials, Manchester Institute of Biotechnology, Faculty of Science and Engineering, The University of Manchester, Manchester M13 9PL, UK.

出版信息

Molecules. 2022 Nov 15;27(22):7901. doi: 10.3390/molecules27227901.

DOI:10.3390/molecules27227901
PMID:36432002
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC9698559/
Abstract

Peptide-based hydrogels are of great interest in the biomedical field according to their biocompatibility, simple structure and tunable properties via sequence modification. In recent years, multicomponent assembly of peptides have expanded the possibilities to produce more versatile hydrogels, by blending gelating peptides with different type of peptides to add new features. In the present study, the assembly of gelating P5 peptide SFFSF blended with P21 peptide, SFFSFGVPGVGVPGVGSFFSF, an elastin-inspired peptides or, alternatively, with FF dipeptide, was investigated by oscillatory rheology and different microscopy techniques in order to shed light on the nanotopologies formed by the self-assembled peptide mixtures. Our data show that, depending on the added peptides, cooperative or disruptive assembly can be observed giving rise to distinct nanotopologies to which correspond different mechanical properties that could be exploited to fabricate materials with desired properties.

摘要

基于肽的水凝胶因其生物相容性、简单的结构以及通过序列修饰可调节的性质,在生物医学领域引起了极大的关注。近年来,通过将凝胶肽与不同类型的肽混合,多组分组装肽扩展了生产更多多功能水凝胶的可能性,从而为水凝胶添加新的特性。在本研究中,通过振荡流变学和不同的显微镜技术研究了凝胶肽 P5 SFFSF 与弹性蛋白模拟肽 P21 SFFSFGVPGVGVPGVGSFFSF 或 FF 二肽的组装,以阐明自组装肽混合物形成的纳米拓扑结构。我们的数据表明,根据添加的肽的不同,可以观察到协同或破坏组装,从而产生不同的纳米拓扑结构,对应不同的机械性能,这些性能可用于制造具有所需性能的材料。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3700/9698559/0f325a876bb3/molecules-27-07901-g010.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3700/9698559/a830461af9c4/molecules-27-07901-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3700/9698559/58673fe1e57e/molecules-27-07901-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3700/9698559/018a19004a59/molecules-27-07901-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3700/9698559/efa7b8416a43/molecules-27-07901-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3700/9698559/73b2682c8769/molecules-27-07901-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3700/9698559/f7518bd9d896/molecules-27-07901-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3700/9698559/5feec97f695a/molecules-27-07901-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3700/9698559/e987b4badf28/molecules-27-07901-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3700/9698559/ada8779ce513/molecules-27-07901-g009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3700/9698559/0f325a876bb3/molecules-27-07901-g010.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3700/9698559/a830461af9c4/molecules-27-07901-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3700/9698559/58673fe1e57e/molecules-27-07901-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3700/9698559/018a19004a59/molecules-27-07901-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3700/9698559/efa7b8416a43/molecules-27-07901-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3700/9698559/73b2682c8769/molecules-27-07901-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3700/9698559/f7518bd9d896/molecules-27-07901-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3700/9698559/5feec97f695a/molecules-27-07901-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3700/9698559/e987b4badf28/molecules-27-07901-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3700/9698559/ada8779ce513/molecules-27-07901-g009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3700/9698559/0f325a876bb3/molecules-27-07901-g010.jpg

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本文引用的文献

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