Investigation on the interaction between triclosan and bovine serum albumin by spectroscopic methods.
Triclosan
bovine serum albumin
molecular docking
spectroscopic techniques
Journal
Journal of environmental science and health. Part. B, Pesticides, food contaminants, and agricultural wastes
ISSN: 1532-4109
Titre abrégé: J Environ Sci Health B
Pays: England
ID NLM: 7607167
Informations de publication
Date de publication:
2020
2020
Historique:
pubmed:
28
8
2019
medline:
14
4
2020
entrez:
28
8
2019
Statut:
ppublish
Résumé
Multi-spectroscopic and molecular docking methods were used to study the interaction between triclosan (TCS) and bovine serum albumin (BSA). The results indicated that the fluorescence quenching of BSA by TCS was due to the formation of TCS-BSA complex through static quenching. This result was also demonstrated by time-resolved fluorescence experiment. The binding constants and number of binding sites between TCS and BSA were 1.30 × 10
Identifiants
pubmed: 31453744
doi: 10.1080/03601234.2019.1656499
doi:
Substances chimiques
Anti-Infective Agents, Local
0
Serum Albumin, Bovine
27432CM55Q
Triclosan
4NM5039Y5X
Types de publication
Journal Article
Video-Audio Media
Langues
eng
Sous-ensembles de citation
IM