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Titolo:
Collision-induced dissociation of ring-opened cyclic depsipeptides with a guanidino group by electrospray ionization/ion trap mass spectrometry
Autore:
Kuroda, J; Fukai, T; Nomura, T;
Indirizzi:
Toho Univ, Fac Pharmaceut Sci, Funabashi, Chiba 2748510, Japan Toho Univ Funabashi Chiba Japan 2748510 , Funabashi, Chiba 2748510, Japan
Titolo Testata:
JOURNAL OF MASS SPECTROMETRY
fascicolo: 1, volume: 36, anno: 2001,
pagine: 30 - 37
SICI:
1076-5174(200101)36:1<30:CDORCD>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
COPIAMYCIN; PEPTIDES;
Keywords:
collision-induced dissociation mass spectrometry; electrospray ionization/ion trap mass spectrometry; fragment ion; depsipeptide; LI-F antibiotics;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
29
Recensione:
Indirizzi per estratti:
Indirizzo: Fukai, T Toho Univ, Fac Pharmaceut Sci, 2-2-1 Miyama, Funabashi, Chiba 2748510, Japan Toho Univ 2-2-1 Miyama Funabashi Chiba Japan 2748510 48510, Japan
Citazione:
J. Kuroda et al., "Collision-induced dissociation of ring-opened cyclic depsipeptides with a guanidino group by electrospray ionization/ion trap mass spectrometry", J MASS SPEC, 36(1), 2001, pp. 30-37

Abstract

The characteristics shown in the electrospray ionization/ion trap mass spectra of ring-opened LI-F antibiotics (cyclic depsihexapeptides with a 15-guanidino-3-hydroxypentadecanoic group as a side-chain) were examined. Collision-induced dissociation (CID) MS of protonated molecules of the depsipeptides produced many fragment ions. Most of these fragment ions contained information for determining the amino acid sequences of antifungal antibiotics. The fragment ions were classified into six groups (b(n), B-n, B-n', beta (n), y(n) and Y-n). According to MS3 spectra, the B-n, B-n' and beta (n) ions can be considered to be derived with a cleavage at each CO-NH in the peptide bonds of [MH - NH3](+), [MH - NH3 - OH](+) and [MH - NH3 - 2H(2)O](+), respectively, in ion trap MS. Losses of NH3 and H2O from the amino acid residues of the depsipeptides in ion trap MS are likely to be smaller than those from the side-chain. The measurements with electrospray ionization (ESI)/ion trap MS of depsipeptides with a side chain containing polar groups mayprovide useful information for structural determination. Copyright (C) 2001 John Wiley & Sons, Ltd.

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Documento generato il 29/03/20 alle ore 09:07:41