PROFLAVINE-SENSITIZED PHOTOOXIDATION OF TRYPTOPHAN AND RELATED PEPTIDES

Autor:	G. Galiazzo, E. Scoffone, G. Iori, C. A. Banassi
Rok vydání:	2008
Předmět:	chemistry.chemical_classification Stereochemistry Cystine Tryptophan Biological activity General Medicine Biochemistry Amino acid chemistry.chemical_compound chemistry Physical and Theoretical Chemistry Tyrosine Proflavine Kynurenine Histidine
Zdroj:	Photochemistry and Photobiology. 6:857-866
ISSN:	1751-1097 0031-8655
DOI:	10.1111/j.1751-1097.1967.tb09650.x
Popis:	— The photodynamic action of proflavine on the amino acids cystine, rnethionine, tyrosine, histidine, tryptophan and related peptides was tested in anhydrous formic and acetic acids. Only rnethionine and tryptophan were found to be photooxidized: the former, whether free or bound in a polypeptide chain, is quantitatively converted to methioninesulphoxide; the latter, when free, is fragmented to several compounds, which may be divided into two main classes: melanines and kynurenine derivatives. Whereas masking the carboxyl group of tryptophan has no effect on the photooxidation products, N-substituted derivatives of tryptophan are converted in high yields to the corre-sponding kynurenine compounds. The possible applications of the method to biologically active polypeptides are discussed.
Databáze:	OpenAIRE
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