Interaction of chlorpropamide with serum albumin: Effect on advanced glycated end (AGE) product fluorescence.
AGE product
Chlorpropamide
Diabetes
Fluorescence quenching
Serum albumin
Journal
Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy
ISSN: 1873-3557
Titre abrégé: Spectrochim Acta A Mol Biomol Spectrosc
Pays: England
ID NLM: 9602533
Informations de publication
Date de publication:
05 Jan 2019
05 Jan 2019
Historique:
received:
09
06
2018
revised:
17
08
2018
accepted:
27
08
2018
pubmed:
7
9
2018
medline:
24
12
2018
entrez:
7
9
2018
Statut:
ppublish
Résumé
Carrier proteins like bovine or human serum albumin (BSA and HSA, respectively) are prone to glycation as compared to the other available proteins. In this study, reducing sugars such as l-arabinose (ara), d-(-) galactose (gal) and d-(-) fructose (fru) were used to create model glycated serum albumins and binding ability of these with well-known antidiabetic drug chlorpropamide (CPM) was monitored. Fluorescence quenching experiment revealed that interaction of CPM with native as well as glycated albumins undergoes through a ground state complex formation. CPM binds strongly to glycated HSA with arabinose (gHSA
Identifiants
pubmed: 30189383
pii: S1386-1425(18)30831-X
doi: 10.1016/j.saa.2018.08.055
pii:
doi:
Substances chimiques
Drug Carriers
0
Glycation End Products, Advanced
0
Hypoglycemic Agents
0
Serum Albumin
0
Chlorpropamide
WTM2C3IL2X
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
569-577Informations de copyright
Copyright © 2018 Elsevier B.V. All rights reserved.