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相反电荷短肽的共组装形成了具有明确结构的超分子水凝胶。

Coassembly of oppositely charged short peptides into well-defined supramolecular hydrogels.

机构信息

Key Laboratory of Biomedical Polymers of Ministry of Education & Department of Chemistry, Wuhan University, Wuhan 430072, PR China.

出版信息

J Phys Chem B. 2010 Feb 25;114(7):2365-72. doi: 10.1021/jp9102417.

Abstract

Two types of oppositely charged short peptides comprised of a hydrophobic N-fluorenyl-9-methoxycarbonyl (FMOC) tail and a peptide backbone were designed and prepared via a standard solid phase peptide (SPPS) technique. When mixing these two oppositely charged peptides in water at a neutral pH, a supramolecular hydrogel with fibroid morphology could be formed via the electrostatic attraction triggered coassembly. The spectroscopic techniques indicated that the hydrogen bonding interactions of the peptide backbones resulted in the formation of antiparallel beta-sheet like superstructure, and the fluorenyl rings connected to the peptide backbones were thus pi-stacked with each other through an antiparallel fashion in the formed nanofibers. Due to the weak flexibility of peptide chains and steric hindrance of rigid fluorenyl rings during the initial process of the coassembly of the oppositely charged peptides, a relatively slow self-assembly was presented, and a higher concentration of the oppositely charged peptides was necessary for this supramolecular hydrogel formation. The strategy demonstrated in this study can be developed as a convenient approach for different types of short peptides to coassemble into a supramolecular hydrogel with multiple functions for the biomedical applications.

摘要

两种带相反电荷的短肽由疏水性 N-芴甲氧羰基(FMOC)尾和肽骨架组成,通过标准固相肽(SPPS)技术设计和制备。当将这两种带相反电荷的肽在中性 pH 的水中混合时,可以通过静电吸引触发共组装形成纤维状形态的超分子水凝胶。光谱技术表明,肽骨架的氢键相互作用导致形成反平行的β-折叠样超结构,并且连接到肽骨架上的芴基环通过反平行方式彼此堆积在形成的纳米纤维中。由于在带相反电荷的肽共组装的初始过程中肽链的柔韧性较弱且刚性芴基环的空间位阻较大,因此呈现出相对较慢的自组装,并且需要更高浓度的带相反电荷的肽来形成这种超分子水凝胶。本研究中展示的策略可以发展成为一种方便的方法,用于不同类型的短肽共组装成具有多种功能的超分子水凝胶,用于生物医学应用。

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