Binding and conformational changes of human serum albumin upon interaction with 4-aminoantipyrine studied by spectroscopic methods and cyclic voltammetry.
Spectrochim Acta A Mol Biomol Spectrosc
; 124: 397-403, 2014 Apr 24.
Article
in En
| MEDLINE
| ID: mdl-24508878
ABSTRACT
The interactions of 4-aminoantipyrine (AAP) with human serum albumin (HSA) have been studied by UV-visible spectroscopy, fluorescence spectroscopy and cyclic voltammetry. The binding of 4-aminoantipyrine quenches the HSA fluorescence, revealing a 11 interaction with a binding constant of about 10(5) M(-1). The experimental results showed that AAP effectively quenched the intrinsic fluorescence of HSA via dynamic type of quenching. In addition, according to the synchronous fluorescence spectra of HSA in presence of 4-aminoantipyrine, the tryptophan residue of the proteins are most perturbed by the binding process. The number of binding sites, the binding constant, site probe study, some common metal ions effect and the thermodynamic parameters were calculated.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Serum Albumin
/
Ampyrone
/
Electrochemical Techniques
Limits:
Humans
Language:
En
Journal:
Spectrochim Acta A Mol Biomol Spectrosc
Journal subject:
BIOLOGIA MOLECULAR
Year:
2014
Document type:
Article
Affiliation country: