期刊
JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY
卷 15, 期 8, 页码 1156-1160出版社
SPRINGER
DOI: 10.1016/j.jasms.2004.04.023
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资金
- NICHD NIH HHS [HD13527] Funding Source: Medline
- NIDDK NIH HHS [DK26741] Funding Source: Medline
- PHS HHS [0216654] Funding Source: Medline
The ability of MALDI-MS to analyze photolabile arylazido peptide derivatives was investigated. Peptides containing UV-Iabile p-azidobenzoyl groups were subjected to MALDI-MS analysis in a variety of matrices. As standard MALDI-MS employs a UV laser (337 nm), we investigated conditions that would allow detection of the intact molecule ions for these light-sensitive peptides. When using alpha-cyano-4-hydroxycinnamic acid (ACHC) or 2,5 dihydroxybenzoic acid (DHB) as the matrix, photoinduced degradation products were prevalent. In contrast, when employing the matrix sinapinic acid, the intact molecule ion corresponding with the azido peptide was the predominant signal. The protection of photolabile azido derivatives correlates with the UV absorbance properties of the matrix employed, i.e., sinapinic acid, which exhibits a strong absorbance near 337 nm, most efficiently protects the azido derivative from photodegradation. (C) 2004 American Society for Mass Spectrometry.
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