Please use this identifier to cite or link to this item: https://repositorio.unifesp.br/handle/11600/42813
Title: Peptide Structure Modifications: Effect of Radical Species Generated by Controlled Gamma Ray Irradiation Approach
Authors: Vieira, Renata de Freitas Fischer [UNIFESP]
Nardi, Daniela Teves [UNIFESP]
Nascimento, Nanci
Rosa, Jose Cesar [UNIFESP]
Nakaie, Clovis Ryuichi [UNIFESP]
Universidade Federal de São Paulo (UNIFESP)
Universidade de São Paulo (USP)
Keywords: gamma radiation
peptide
mass spectrometry
alpha-melanocyte-stimulating hormone
bradykinin
substance P
Issue Date: 1-Apr-2013
Publisher: Pharmaceutical Soc Japan
Citation: Biological & Pharmaceutical Bulletin. Tokyo: Pharmaceutical Soc Japan, v. 36, n. 4, p. 664-675, 2013.
Abstract: The present work aimed at evaluating the radiolysis effect upon a set of peptides, most of them involved in physiological functions. To generate reactive radical species, a Co-60 source (up to 15 kGy) was used for controlled gamma irradiation of some peptide solutions including derivatives attaching the stable free radical Toac (2,2,6,6-tetramethypiperidine-1-oxyl-4-amino-4-carboxylic acid). Regardless of the peptide sequence, a nonlinear and progressive degradation of a total of nine peptides was detected. The results were interpreted in the light of the half-life dose (D-1/2) parameter which represents the dose necessary for 50% peptide structure degradation. The vasoactive angiotensin II (AngII)'s analogue Ang-(1-7) showed greater stability towards gamma ray radiation than bradykinin (BK), Toac(0)-BK, Pro(4)-BK (D-1/2 around 4 and 2 kGy, respectively) which decreased to about 0.5-1.0 kGy in the case of acetyl-alpha-melanocyte-stimulating hormone (Aca-MSH) and substance P (SP). In terms of peptide structural modifications, the data acquired from different analytical methods suggested a Phe to Tyr (or its ortho and/or meta isomers) transformation as a consequence of the hydroxyl moiety insertion. Noteworthy, this effect seemed to be position-dependent as only Phe located at or near the C-terminal portion seemed to display this transformation. In contrast, Met is comparatively more easily oxidized, thus allowing to conclude that gamma irradiation may induce a complex position and/or sequence-dependent effect on peptides. As previously applied for BK, some irradiated peptides were submitted to their by-products purification, indeed a complementary target of the present approach for development of uncommon analogues for further structure-function investigation.
URI: http://repositorio.unifesp.br/11600/42813
ISSN: 0918-6158
Other Identifiers: http://doi.org/10.1248/bpb.b12-01036
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