一种抗冻多肽与冰结合的模型。

A model for binding of an antifreeze polypeptide to ice.

作者信息

Wen D, Laursen R A

机构信息

Department of Chemistry, Boston University, Massachusetts 02215.

出版信息

Biophys J. 1992 Dec;63(6):1659-62. doi: 10.1016/S0006-3495(92)81750-2.

DOI:10.1016/S0006-3495(92)81750-2

PMID:1489916

原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1262283/

Abstract

A model is proposed, based on recent peptide analog and ice crystal etching studies, whereby an alanine-rich, alpha-helical antifreeze polypeptide (AFP) from the winter flounder inhibits the growth of ice crystals by hydrogen bonding of Thr, Asn, and Asp side chains in a specific pattern to the [2021] hexagonal bipyramidal planes of ice. It is further suggested that this mode of binding is unidirectional, maximizing opportunities for packing of AFPs on the ice surface, and that ice crystal growth inhibition occurs by a two-step mechanism involving hydrogen bonding and hydrophobic interpeptide interactions.

摘要

基于最近的肽类似物和冰晶蚀刻研究，提出了一个模型，据此，来自冬季比目鱼的富含丙氨酸的α-螺旋抗冻多肽（AFP）通过苏氨酸、天冬酰胺和天冬氨酸侧链以特定模式与冰的[2021]六方双锥面形成氢键来抑制冰晶生长。还进一步表明，这种结合模式是单向的，使AFP在冰表面堆积的机会最大化，并且冰晶生长抑制是通过涉及氢键和疏水肽间相互作用的两步机制发生的。