Self-assembling peptide inspired by a barnacle underwater adhesive protein
Self-assembling peptide inspired by a barnacle underwater adhesive protein
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DOI：
10.1021/bm0612236
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发表时间：
2007-06-01
影响因子：
6.2
通讯作者：
Kamino, Kei
中科院分区：
文献类型：
--
作者：
Nakano, Masahiro;Shen, Jian-Ren;Kamino, Kei
水下生物粘附剂通常包含为自组装提供分子基础的多蛋白质复合物。我们在这里报告一类新的自组装肽的灵感来自20 kDa的藤壶水泥蛋白。对化学合成的24-残基肽的研究表明，（1）它在加入盐时经历不可逆的自组装，（2）自组装在接近海水的盐浓度下开始，具有非共价分子间相互作用，（3）自组装材料类似于交织纳米丝的宏观膜，（4）在碱性pH范围内孵育形成肽分子的分子内二硫键，从而引发分子的构象变化，和（5）结构单元的构象变化促进了构象的形成，导致显示出具有直径约为200 nm的限定孔的三维网状介观结构。该肽可能为进一步开发基于肽的材料提供合适的基础。
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.