Deciphering the Conformations of Glutathione Oxidized Peptide: A Comparative NMR Study in Solution and Solid-State Environments.
GSSG
NOE
peptide conformation
solid‐state NMR
solution NMR
Journal
Magnetic resonance in chemistry : MRC
ISSN: 1097-458X
Titre abrégé: Magn Reson Chem
Pays: England
ID NLM: 9882600
Informations de publication
Date de publication:
16 Oct 2024
16 Oct 2024
Historique:
revised:
05
08
2024
received:
16
04
2024
accepted:
27
09
2024
medline:
17
10
2024
pubmed:
17
10
2024
entrez:
17
10
2024
Statut:
aheadofprint
Résumé
Glutathione (GSH) and its oxidized dimer (GSSG) play an important role in living systems as an antioxidant, balancing the presence of reactive oxygen species (ROS). The central thiol (-S-S-) bond in GSSG can undergo free rotation, providing multiple conformations with respect to the S-S bridge. The six titratable sites of GSSG, which are influenced by pH variations, affect these conformations in solution, whereas in solids, additionally crystal packing effects come into play. In view of differing reports about the structure of GSSG in literature, we have here conducted an extensive reexamination of its conformations using NMR, and contrasting results have been obtained for solution and solid state. In solution, the existence of more than one antiparallel orientation of the monomer unit with different hydrogen bonding schemes has been indicated by NOE and amide temperature coefficient results. On the other hand, in the solid-state, a
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : CSIR
Organisme : Emeritus Scientist
ID : 21(1018)/15/EMR-II
Organisme : SRF
Organisme : DST INSPIRE
Informations de copyright
© 2024 John Wiley & Sons A/S. Published by John Wiley & Sons Ltd.
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