Multi-Spectroscopic and Theoretical Analysis on the Interaction between Human Serum Albumin and a Capsaicin Derivative-RPF101.
Biomolecules
; 8(3)2018 08 23.
Article
en En
| MEDLINE
| ID: mdl-30142945
ABSTRACT
The interaction between the main carrier of endogenous and exogenous compounds in the human bloodstream (human serum albumin, HSA) and a potential anticancer compound (the capsaicin analogue RPF101) was investigated by spectroscopic techniques (circular dichroism, steady-state, time-resolved, and synchronous fluorescence), zeta potential, and computational method (molecular docking). Steady-state and time-resolved fluorescence experiments indicated an association in the ground state between HSARPF101. The interaction is moderate, spontaneous (ΔG° < 0), and entropically driven (ΔS° = 0.573 ± 0.069 kJ/molK). This association does not perturb significantly the potential surface of the protein, as well as the secondary structure of the albumin and the microenvironment around tyrosine and tryptophan residues. Competitive binding studies indicated Sudlow's site I as the main protein pocket and molecular docking results suggested hydrogen bonding and hydrophobic interactions as the main binding forces.
Palabras clave
Texto completo:
1
Bases de datos:
MEDLINE
Asunto principal:
Capsaicina
/
Simulación del Acoplamiento Molecular
/
Albúmina Sérica Humana
Límite:
Humans
Idioma:
En
Revista:
Biomolecules
Año:
2018
Tipo del documento:
Article
País de afiliación:
Brasil