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Chromophore effect in photodissociation at 266 nm of protonated peptides generated by matrix‐assisted laser desorption ionization (MALDI)
Author(s) -
Oh Joo Yeon,
Moon Jeong Hee,
Kim Myung Soo
Publication year - 2005
Publication title -
journal of mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 1076-5174
DOI - 10.1002/jms.866
Subject(s) - chemistry , chromophore , photodissociation , protonation , peptide , dissociation (chemistry) , photochemistry , mass spectrometry , residue (chemistry) , matrix assisted laser desorption/ionization , ion , peptide fragment , stereochemistry , desorption , organic chemistry , chromatography , biochemistry , adsorption
Abstract Chromophore effect in the photodissociation of protonated peptides at 266 nm was investigated using synthetic peptides with the sequence RGGXR where X was a phenylalanyl(F), tyrosyl(Y), cysteinyl(C), glycyl(G), seryl(S), or histidyl(H) residue. The peptides with an F or Y residue dissociated efficiently. Fragment ions due to cleavages at either end of the chromophore were especially prominent just as for the peptide with a tryptophanyl residue reported previously.1Photodissociation was observed even for the peptides without any noticeable chromophore at 266 nm. Here, dissociation at all the peptide bonds was almost equally prominent. Photodissociation of the protonated angiotensin I was investigated using the spectral correlation rules observed in the model systems. Role of the chromophores and the plausible mechanisms involved are discussed. Copyright © 2005 John Wiley & Sons, Ltd.