Effect of triazole-tryptophan hybrid on the conformation stability of bovine serum albumin.
Luminescence
; 33(3): 464-474, 2018 May.
Article
em En
| MEDLINE
| ID: mdl-29314579
ABSTRACT
The effect of a potent antimicrobial compound bearing 1,2,3-triazole core and a tryptophan tail, triazole-tryptophan hybrid (TTH), with bovine serum albumin (BSA) have been explored using various spectroscopic and molecular docking methods. Studies revealed that TTH strongly quenches the intrinsic fluorophore of BSA by a static quenching mechanism. Time-resolved fluorescence spectra further confirmed the involvement of static quenching for TTH-BSA system. The calculated thermodynamic parameters; ΔH, ΔS, and ΔG showed that the binding process was spontaneous, exothermic and entropy driven. Synchronous fluorescence, three-dimensional (3D) fluorescence and circular dichroism data revealed that TTH induces the structural alteration in BSA and enhances its stability. In silico study of TTH-BSA system showed that it binds with BSA at the site I of subdomain IIA. Both the experimental and in silico study showed that the hydrophobic and electrostatic interactions play a major role in TTH-BSA binding.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Triazóis
/
Triptofano
/
Soroalbumina Bovina
Idioma:
En
Revista:
Luminescence
Assunto da revista:
BIOFISICA
/
BIOQUIMICA
Ano de publicação:
2018
Tipo de documento:
Article
País de afiliação:
Índia