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Titolo:
Sequencing cyclic peptide inhibitors of mammalian ribonucleotide reductaseby electrospray ionization mass spectrometry
Autore:
Lin, SH; Liehr, S; Cooperman, BS; Cotter, RJ;
Indirizzi:
Johns Hopkins Univ, Sch Med, Dept Pharmacol & Mol Sci, Baltimore, MD 21205USA Johns Hopkins Univ Baltimore MD USA 21205 Mol Sci, Baltimore, MD 21205USA Univ Penn, Dept Chem, Philadelphia, PA 19104 USA Univ Penn Philadelphia PA USA 19104 Dept Chem, Philadelphia, PA 19104 USA
Titolo Testata:
JOURNAL OF MASS SPECTROMETRY
fascicolo: 6, volume: 36, anno: 2001,
pagine: 658 - 663
SICI:
1076-5174(200106)36:6<658:SCPIOM>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
COLLISION-INDUCED DISSOCIATION; AMINO-ACID-SEQUENCE; GAS-PHASE; ACTIVATED DECOMPOSITION; IONS ADJACENT; R1 SUBUNIT; FRAGMENTATION; HEPTAPEPTIDE; MICROCYSTINS; CHARGE;
Keywords:
cyclic peptide; mammalian ribonucleotide reductase; electrospray ionization mass spectrometry; collision-induced dissociation; charge-remote fragmentation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: Cotter, RJ Johns Hopkins Univ, Sch Med, Dept Pharmacol & Mol Sci, 725 N Wolfe St, Baltimore, MD 21205 USA Johns Hopkins Univ 725 N Wolfe St BaltimoreMD USA 21205 05 USA
Citazione:
S.H. Lin et al., "Sequencing cyclic peptide inhibitors of mammalian ribonucleotide reductaseby electrospray ionization mass spectrometry", J MASS SPEC, 36(6), 2001, pp. 658-663

Abstract

Mammalian ribonucleotide reductase (mRR) is a potential target for cancer intervention. A series of lactam-bridged cyclic peptide inhibitors (1-9) ofmRR have been synthesized and tested in previous work. These inhibitors consist of cyclic and linear regions, causing their mass spectral characterization to be a challenge. We determined the fragmentation mechanism of cyclic peptides 1-9 using an ion-trap mass spectrometer equipped with an ESI source. Low-energy collision-induced dissociation of sodiated cyclic peptides containing linear branches follows a general pathway. Fragmentation of the linear peptide region produced mainly a and b ions. The ring peptide regionwas more stable and ring opening required higher collision energy, mainly occurring at the amide bond adjacent to the lactam bridge. The sodium ion, which bound to the carbonyl oxygen of the lactam bridge, acted as a fixed charge site and directed a charge-remote, sequence-specific fragmentation ofthe ring-opened peptide. Amino acid residues were cleaved sequentially from the C-terminus to the N-terminus. Our findings have established a new wayto sequence cyclic peptides containing a lactam bridge based on charge-remote fragmentation. This methodology will permit unambiguous identification of high-affinity ligands within cyclic peptide libraries. Copyright (C) 2001 John Wiley & Sons, Ltd.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/03/20 alle ore 00:47:21