α-螺旋抗冻肽的合理设计

Rational design of alpha-helical antifreeze peptides.

作者信息

Kuiper M J, Fecondo J V, Wong M G

机构信息

School of Engineering and Science, Swinburne University of Technology, Hawthorn, Victoria, Australia.

出版信息

J Pept Res. 2002 Jan;59(1):1-8. doi: 10.1046/j.1397-002x.2001.00001.x.

DOI:10.1046/j.1397-002x.2001.00001.x

PMID:11906602

Abstract

The alanine-rich alpha-helical antifreeze protein from the winter flounder Pseudopleuronectes americanus adsorbs to specific planes of ice guided by an ice lattice match to threonine residues regularly spaced 16.6 A apart. We report here that by redesigning the winter flounder antifreeze peptide to incorporate a 27.1-A spacing between putative 'ice-binding' threonines, the deduced binding alignment of the helical molecule on the ice lattice is changed from the Miller indices directional vector [1102 ] to [2203 ]. Subsequent ice-binding characteristics are altered, including changes in adsorption specificity, decreases in thermal hysteresis activity and the formation of rotated hexagonal bipyramid ice crystal morphology.

摘要

来自美洲拟庸鲽的富含丙氨酸的α-螺旋抗冻蛋白会吸附到特定的冰面上，这一过程由与苏氨酸残基的冰晶格匹配所引导，这些苏氨酸残基以16.6埃的间隔规则排列。我们在此报告，通过重新设计美洲拟庸鲽抗冻肽，使假定的“冰结合”苏氨酸之间的间距为27.1埃，螺旋分子在冰晶格上的推导结合排列从米勒指数方向矢量[1102]变为[2203]。随后冰结合特性发生改变，包括吸附特异性的变化、热滞活性的降低以及旋转六方双锥冰晶形态的形成。