Akademik Veri Yönetim Sistemi
INTERNATIONAL HAZAR SCIENTIFIC RESEARCH CONGRESS - III, Azerbaycan, 07 Ocak 2022
As known that endogenous ligands
and drugs bind to proteins, and it has been emphasized in the literature that
the interactions of drugs with not only nucleic acids but also proteins are
important in the understand therapeutic
efficacy of drugs. Moreover, the mentioned mechanism has important role to
elucidate biological activity of drugs. In the present study, studies on
drug-protein interactions in the literature were investigated and reviewed. Albumine
is the most abundant protein in human plasma and the human serum albumin has
great similarity with bovine serum albumin the investigated interaction studies
were performed with human serum albumin
(HSA) or bovine serum albumin (BSA). The various spectroscopic methods as like Ultraviolet (Ultraviolet) and
Visible Region (UV-GB) Spectroscopy, Fluorescence Spectroscopy, and Circular
Dichroism (CD) Spectroscopy have been reported in order to elucidate
protein-drug complexation mechanism. The
effect of ionic strength, temperature or pH were examined to the complex
formation constants of BSA/HSA-Drugs.
Accordingly, The Complex formation constants remained at different
temperatures and ionic concentrations, Stern-Volmer graphs, Van't Hoff
equations were obtained, and interpretations were made for thermodynamic parameters
between HSA and BSA proteins and drug molecules. Apart from this, it has been
observed that the energy change of these systems is determinant in determining
the ineffective forces of the drug-protein binding.
Keywords: Drugs, Drug-Protein
Bindings, Thermodynamic Parameters