albumin - publications

Predict more albumin - ligand interactions now!


1. Phys Chem Chem Phys. 2012 Feb 21. [Epub ahead of print]

Deciphering the role of pH in the binding of Ciprofloxacin Hydrochloride to
Bovine Serum Albumin.

Anand U, Kurup L, Mukherjee S.

Department of Chemical Sciences, Indian Institute of Science Education and
Research Bhopal, ITI Campus (Gas Rahat) Building, Govindpura, Bhopal 462 023,
Madhya Pradesh, India. saptarshi@iiserbhopal.ac.in.

The effect of the added fluoroquinolone, Ciprofloxacin Hydrochloride (CpH), on
structural properties of Bovine Serum Albumin (BSA) was investigated by Circular
Dichroism (CD), steady-state, time-resolved and Dynamic Light Scattering (DLS)
spectroscopic approaches. The intrinsic fluorescence of the Tryptophan (Trp)
amino acid residue in the globular protein BSA was made use of and the effect of
pH at two different temperatures was thoroughly investigated. CD results indicate
that CpH induces some structural changes in BSA and this has been well-supported
by steady-state, lifetime and DLS data. The fluorescence intensity of Trp
gradually decreases with the rise in concentration of CpH and we have
conclusively proved that at pH 7.4 and 9.2, the mechanism of fluorescence
quenching is mostly dynamic in nature, whereas at pH 4.5 mainly static quenching
is operational. Thermodynamic parameters have been studied to rationalize the
nature of binding of CpH to BSA, and we have concluded that hydrophobic and van
der Waals forces play an important role in the process of drug-protein
interaction at three different pH values. The lifetime of Trp was found to
decrease with the rise in CpH concentration and the percentage reduction in
lifetime was found to be a function of the pH of the medium under investigation.

PMID: 22354288 [PubMed - as supplied by publisher]