Electron transfer dissociation reveals changes in the cleavage frequencies of backbone bonds distant to amide-to-ester substitutions in polypeptides.
J Am Soc Mass Spectrom
; 22(11): 1953-7, 2011 Nov.
Article
em En
| MEDLINE
| ID: mdl-21952783
ABSTRACT
Interrogation of electron transfer dissociation (ETD) mass spectra of peptide amide-to-ester backbone bond substituted analogues (depsipeptides) reveals substantial differences in the entire backbone cleavage frequencies. It is suggested that the point permutation of backbone bonds leads to changes in the predominant ion structures by removal/weakening of specific hydrogen bonding. ETD responds to these changes by redistributing the cleavage frequencies of the peptide backbone bonds. In comparison, no distinction between depsi-/peptide was observed using collision-activated dissociation, which is consistent with a general unfolding and elimination of structural information of these ions. These results should encourage further exploration of depsipeptides for gas-phase structural characterization.
Texto completo:
1
Bases de dados:
MEDLINE
Assunto principal:
Peptídeos
/
Espectrometria de Massas
/
Amidas
Idioma:
En
Revista:
J Am Soc Mass Spectrom
Ano de publicação:
2011
Tipo de documento:
Article
País de afiliação:
Dinamarca