期刊
CHEMICAL PHYSICS LETTERS
卷 478, 期 4-6, 页码 249-253出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.cplett.2009.07.058
关键词
-
资金
- National Institutes of Health [GM-065978, RR-01348]
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. (C) 2009 Elsevier B. V. All rights reserved.
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