Optical fingerprinting of peptides using two-dimensional infrared spectroscopy: Proof of principle

被引:29
|
作者
Fournier, Frederic [1 ]
Gardner, Elizabeth M. [1 ]
Guo, Rui [1 ]
Donaldson, Paul M. [1 ]
Barter, Laura M. C. [1 ]
Palmer, D. Jason [2 ]
Barnett, Chris J. [1 ]
Willison, Keith R. [3 ]
Gould, Ian R. [1 ]
Klug, David R. [1 ]
机构
[1] Univ London Imperial Coll Sci Technol & Med, Dept Chem, Mol Dynam Res Grp, London SW7 2AZ, England
[2] Univ Florence, European Lab Nonlinear Spectroscopy, I-50019 Florence, Italy
[3] Ctr Cellular & Mol Biol, Canc Res UK, Chester Beatty Labs, Inst Canc Res, London SW3 6JB, England
基金
英国工程与自然科学研究理事会;
关键词
two-dimensional infrared spectroscopy; 2DIR; proteomics; peptides; phenylalanine; tyrosine; protein fingerprinting; amino acid;
D O I
10.1016/j.ab.2007.11.009
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
We employ a particular form of two-dimensional infrared four-wave mixing (2DIR FWM) as a vibrational spectroscopic tool to quantify the amino acid content of a number of peptides. Vibrational features corresponding to ring modes of the aromatic groups of phenylalanine (Phe) and tyrosine (Tyr), as well as a methylene mode that is used as an internal reference, are identified. We show that the ratios of the integrated intensities, and the amplitudes, of the aromatic peaks of Phe and Tyr relative to the methylene integrated intensity, and amplitude, are proportional to the actual ratio of Phe and Tyr to CH2 in the samples within a precision of +/- 12.5%. This precision is shown to be sufficient to use this form of 2DIR spectroscopy as a possible proteins fingerprinting tool. (C) 2007 Elsevier Inc. All rights reserved.
引用
收藏
页码:358 / 365
页数:8
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