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5-氰基色氨酸作为蛋白质局部水合状态的红外探针

5-Cyanotryptophan as an Infrared Probe of Local Hydration Status of Proteins.

作者信息

Waegele Matthias M, Tucker Matthew J, Gai Feng

机构信息

Department of Chemistry, University of Pennsylvania, 231 South 34 Street, Philadelphia, PA 19104, USA.

出版信息

Chem Phys Lett. 2009 Sep 1;478(4):249-253. doi: 10.1016/j.cplett.2009.07.058.

Abstract

The nitrile (C≡N) stretching vibration is sensitive to environment, making nitrile-derivatized amino acids an increasingly utilized tool to study various biological processes. Herein, we show that the bandwidth of the C≡N stretching vibration of 5-cyanotryptophan is particularly sensitive to water, rendering it an attractive infrared probe of local hydration status. We confirm the utility of this probe in biological applications by using it to examine how the hydration status of individual tryptophan sidechains of an antimicrobial peptide, indolicidin, changes upon peptide binding to model membranes. Furthermore, we show that p-cyanophenylalanine and 5-cyanotryptophan constitute a useful fluorescence energy transfer pair.

摘要

腈基(C≡N)伸缩振动对环境敏感,这使得腈基衍生化的氨基酸成为研究各种生物过程中越来越常用的工具。在此,我们表明5-氰基色氨酸的C≡N伸缩振动带宽对水特别敏感,使其成为局部水合状态的有吸引力的红外探针。我们通过使用该探针来研究抗菌肽吲哚杀菌素的单个色氨酸侧链的水合状态在肽与模型膜结合时如何变化,从而证实了该探针在生物应用中的实用性。此外,我们表明对氰基苯丙氨酸和5-氰基色氨酸构成了一个有用的荧光能量转移对。

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