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受藤壶水下粘附蛋白启发的自组装肽。

Self-assembling peptide inspired by a barnacle underwater adhesive protein.

作者信息

Nakano Masahiro, Shen Jian-Ren, Kamino Kei

机构信息

Marine Biotechnology Institute, 3-75-1 Heita, Kamaishi, Iwate 026-0001, Japan.

出版信息

Biomacromolecules. 2007 Jun;8(6):1830-5. doi: 10.1021/bm0612236. Epub 2007 May 23.

Abstract

An underwater bioadhesive generally comprises a multiprotein complex that provides a molecular basis for self-assembly. We report here a new class of self-assembling peptide inspired by a 20 kDa barnacle cement protein. Studies on the chemically synthesized 24-residue peptide have revealed that (1) it underwent irreversible self-assembly upon the addition of salt, (2) the self-assembly was started at a salt concentration close to that of seawater with noncovalent intermolecular interactions, (3) the self-assembled material resembled a macroscopic membrane of interwoven nanofilaments, (4) incubation in an alkaline pH range formed the intramolecular disulfide bond of a peptide molecule, thus triggering a conformation change of the molecule, and (5) conformational change of the building block promoted the formation of a nanofiber, resulting in the display of a three-dimensional meshlike mesoscopic structure with defined pores having a diameter of approximately 200 nm. The peptide is likely to provide a suitable basis for further development of peptide-based materials.

摘要

水下生物粘合剂通常包含一种多蛋白复合物,该复合物为自组装提供分子基础。我们在此报告一类受20 kDa藤壶粘附蛋白启发的新型自组装肽。对化学合成的24个氨基酸残基的肽的研究表明:(1)加入盐后它会发生不可逆的自组装;(2)自组装在接近海水盐浓度时通过非共价分子间相互作用开始;(3)自组装材料类似于由交织的纳米丝组成的宏观膜;(4)在碱性pH范围内孵育会形成肽分子的分子内二硫键,从而引发分子构象变化;(5)构建模块的构象变化促进了纳米纤维的形成,从而呈现出具有约200 nm直径的确定孔隙的三维网状介观结构。该肽可能为基于肽的材料的进一步开发提供合适的基础。

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