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Titolo:
Location of alkali metal binding sites in endothelin a selective receptor antagonists, cyclo(D-Trp-D-Asp-Pro-D-Val-Leu) and cyclo(D-Trp-D-Asp-Pro-D-Ile-Leu), from multistep collisionally activated decompositions
Autore:
Ngoka, LCM; Gross, ML;
Indirizzi:
Washington Univ, Dept Chem, St Louis, MO 63130 USA Washington Univ St Louis MO USA 63130 , Dept Chem, St Louis, MO 63130 USA
Titolo Testata:
JOURNAL OF MASS SPECTROMETRY
fascicolo: 2, volume: 35, anno: 2000,
pagine: 265 - 276
SICI:
1076-5174(200002)35:2<265:LOAMBS>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
TANDEM MASS-SPECTROMETRY; ACUTE-RENAL-FAILURE; PEPTIDE IONS ADJACENT; NA+-H+ EXCHANGE; DIALKYLGLYCINE DECARBOXYLASE; ELECTROSPRAY IONIZATION; PROTON AFFINITIES; CYCLIC-PEPTIDES; ACID-RESIDUES; CONFORMATION;
Keywords:
endothelin A selective receptor antagonists; alkali metal binding sites; multistep collisionally activated decomposition;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
72
Recensione:
Indirizzi per estratti:
Indirizzo: Gross, ML Washington Univ, Dept Chem, 1 Brookings Dr,Campus Box 1134, St Louis, MO 63130 USA Washington Univ 1 Brookings Dr,Campus Box 1134 St Louis MO USA 63130
Citazione:
L.C.M. Ngoka e M.L. Gross, "Location of alkali metal binding sites in endothelin a selective receptor antagonists, cyclo(D-Trp-D-Asp-Pro-D-Val-Leu) and cyclo(D-Trp-D-Asp-Pro-D-Ile-Leu), from multistep collisionally activated decompositions", J MASS SPEC, 35(2), 2000, pp. 265-276

Abstract

We previously showed by using mass spectrometry that endothelin A selective receptor antagonists BQ123 and JKC301 form novel coordination compounds with sodium ions. This property may underlie the ability of an ETA antagonist to induce net tubular sodium reabsorption in the proximal tubule cells and reverse acute renal failure induced by severe ishemia, We have now defined the metal binding sites on BQ123 and JKC301 by subjecting the metal-containing peptides to multiple stages of collisionally activated decomposition (CAD) in an ion trap mass spectrometer, When submitted to low-energy CAD, the ring opens at the Asp-Pro amide bond. The metal ion, which bonds, inter alia, to the carbonyl oxygen of the proline residue, acts as a fixed chargesite, and directs a charge-remote, sequence-specific fragmentation of the ring-opened peptide. Amino acid residues are sequentially cleaved from the C-terminal end, and the terminal aziridinone structure moves one step toward the N-terminus with each C-terminal amino acid residue removed. These observations are the basis of a new method to sequence cyclic peptides. Amino acid residues are observed as sets of three ions, a(nPD)*, b(nPD)*, and c(nPD)*, where n is the number of amino acid residues in the peptide, Copyright (C) 2000 John Wiley & Sons, Ltd.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/01/20 alle ore 19:23:04