阿什匹林肽被阻留在方解石中，使生物矿物晶体永久无序。

Asprich peptides are occluded in calcite and permanently disorder biomineral crystals.

机构信息

Department of Physics, University of Wisconsin-Madison, 1150 University Avenue, Madison, Wisconsin 53706, USA.

出版信息

J Am Chem Soc. 2010 Aug 25;132(33):11585-91. doi: 10.1021/ja103089r.

PMID:20677733

Abstract

Macromolecules are a minority but important component of the minerals formed by living organisms, or biominerals. The role these macromolecules play at the early stages of biomineral formation, as well as their long-term and long-range effects on the mature biomineral, is poorly understood. A 42-amino acid peptide, asp2, was derived from the Asprich family of proteins. In this study we present X-ray absorption near-edge structure spectroscopy and X-ray photoelectron emission microscopy data from the asp2 peptide, the calcite (CaCO(3)) crystals, and the peptide + crystal composites. The results clearly show that asp2 is occluded in fully formed biomineral crystals and slightly but permanently disorders the crystal structure at short- and long-range distances.

摘要

高分子是生物矿化产物（或生物矿物）中含量较少但却非常重要的组成部分。这些高分子在生物矿化早期形成阶段的作用，以及它们对成熟生物矿物的长期和远距离影响，目前还了解甚少。Asp2 是一种 42 个氨基酸的肽，来源于 Asprich 蛋白家族。在本研究中，我们通过 X 射线吸收近边结构光谱和 X 射线光电子能谱显微镜数据，对 Asp2 肽、方解石（CaCO3）晶体以及肽-晶体复合物进行了研究。结果清楚地表明，Asp2 被包裹在完全形成的生物矿物晶体中，并且在短程和远程距离上都会使晶体结构略有但却永久地发生紊乱。