Literature DB >> 7918693

Open-chain peptides obtained by acidic hydrolytic cleavage of cyclosporin A.

F Magni1, C Arcelloni, R Paroni, I Fermo, P A Bonini, M Del Puppo, A Manzocchi, M Galli Kienle.   

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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Year:  1994        PMID: 7918693     DOI: 10.1002/bms.1200230809

Source DB:  PubMed          Journal:  Biol Mass Spectrom        ISSN: 1052-9306


  1 in total

1.  An unusual side chain C-C cleavage at the MeBmt amino acid in cyclosporin A.

Authors:  A Jegorov; V Havlíček; P Sedmera
Journal:  Amino Acids       Date:  1996-06       Impact factor: 3.520

  1 in total

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