Simultaneous Binding of Folic Acid and Methotrexate to Human Serum Albumin: Insights into the Structural Changes of Protein and the Location and Competitive Displacement of Drugs.

ABSTRACT: Protein structure can be flexible to adopt multiple conformations to house small molecules. In this paper, we have attempted to experimentally figure out how the structure of a transport protein steer the drug-drug competition (DDC) by maintaining the equilibrium distribution of the bound and unbound fractions of drugs. This understanding is an important facet in biophysical and medicinal chemistry to ascertain the effectiveness of drugs. It is important to note that majority of studies involving small-molecule-transport protein interaction aimed at characterizing the binding process, and because these proteins can interact with thousands of molecules, there are hundreds of reports on such interactions. This ultimately led to an impression among the readers that any studies involving serum

SUBMITTER: Panja S 

PROVIDER: S-EPMC6045412 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature