Hydrolysis of cyclosporin A (CsA) was studied in order to clarify the still undefined point of attack of the acidic degradation. Among ether extractable and water-soluble products formed from CsA in HCl, two open-chain peptides were isolated by high-performance liquid chromatography which were identified as the deca- and nonapeptides deriving from CsA through the hydrolytic cleavage of amino acid residue 11 and both residues 11 and 10, respectively. Identification was carried out by fast atom bombardment tandem mass spectrometry.
OPEN-CHAIN PEPTIDES OBTAINED BY ACIDIC HYDROLYTIC CLEAVAGE OF CYCLOSPORINE-A / F. MAGNI, C. ARCELLONI, R. PARONI, I. FERMO, P.A. BONINI, M. DELPUPPO, A. MANZOCCHI, MG KIENLE. - In: BIOLOGICAL MASS SPECTROMETRY. - ISSN 1052-9306. - 23:8(1994 Aug), pp. 514-518.
OPEN-CHAIN PEPTIDES OBTAINED BY ACIDIC HYDROLYTIC CLEAVAGE OF CYCLOSPORINE-A
R. PARONI;
1994
Abstract
Hydrolysis of cyclosporin A (CsA) was studied in order to clarify the still undefined point of attack of the acidic degradation. Among ether extractable and water-soluble products formed from CsA in HCl, two open-chain peptides were isolated by high-performance liquid chromatography which were identified as the deca- and nonapeptides deriving from CsA through the hydrolytic cleavage of amino acid residue 11 and both residues 11 and 10, respectively. Identification was carried out by fast atom bombardment tandem mass spectrometry.
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