Journal
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 97, Issue -, Pages 688-699Publisher
ELSEVIER
DOI: 10.1016/j.ijbiomac.2017.01.047
Keywords
Human hobo transferrin; Amino acids; Lomefloxacin; Spectroscopy; DFT
Funding
- Research Council of the Mashhad Brunch, Islamic Azad University, Mashhad, Iran
Ask authors/readers for more resources
The purpose of this study was to determine how lomefloxacin (LMF) interacts with human holotransferrin (HTF) in the presence of two kinds of essential and nonessential amino acids. The investigations were carried out by fluorescence spectroscopy, zeta potential and molecular modeling techniques under imitated physiological conditions. We were able to determine the number of binding sites, the drug binding affinity to HTF in the presence of essential and nonessential amino acids and the quenching source of HTF. The interaction between HTF with LMF suggested that the microenvironment of the Trp residues was altered causing a strong static fluorescence quenching in the binary and ternary systems. The results pointed at the formation of a complex in the binary and ternary systems which caused an enhancement of the RLS intensity that was analyzed using synchronous fluorescence spectroscopy. The density functional theory (DFT) was employed to determine the amino acid residues on HTF that interacted with LMF. Also, Steric and van der Waals forces as well as the contribution of small amounts of hydrogen bonds were stronger or Tyr 71 in chain (b) than for 128 Trp in chain (a) of HTF. (C) 2017 Elsevier B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available