信号肽肽酶跨膜肽不溶性的研究。

Studies on the insolubility of a transmembrane peptide from signal peptide peptidase.

作者信息

Johnson Erik C B, Kent Stephen B H

机构信息

Institute for Biophysical Dynamics, Department of Biochemistry and Molecular Biology, The University of Chicago, 920 East 58th Street, Chicago, Illinois 60637, USA.

出版信息

J Am Chem Soc. 2006 Jun 7;128(22):7140-1. doi: 10.1021/ja058377y.

DOI:10.1021/ja058377y

PMID:16734449

Abstract

We have undertaken fundamental studies on the solubility properties of a peptide derived from the fourth transmembrane (TM) domain of signal peptide peptidase, a 7-TM intramembrane-cleaving protease. We have found that by disfavoring secondary structure formation we are able to greatly improve the solubility, handling, and purification properties of this peptide. Our findings suggest that preventing secondary structure formation by reversible modification of the polypeptide backbone of hydrophobic transmembrane peptides may be a useful strategy for the total chemical protein synthesis of integral membrane proteins.

摘要

我们对源自信号肽肽酶第四跨膜（TM）结构域的一种肽的溶解性进行了基础研究，信号肽肽酶是一种7次跨膜的膜内裂解蛋白酶。我们发现，通过抑制二级结构的形成，我们能够极大地改善这种肽的溶解性、可操作性和纯化特性。我们的研究结果表明，通过对疏水性跨膜肽的多肽主链进行可逆修饰来防止二级结构的形成，可能是整合膜蛋白全化学合成的一种有用策略。