Spectroscopic Investigation of Procaine Interaction with Human Serum Albumin
Spectroscopic Investigation of Procaine Interaction with Human Serum Albumin
Date
2018-07-05
Authors
Alsamamra, Husain
Khalid, Imtiaz
Alfaqeh, Rania
Farroun, Maryiam
Abuteir, Musa
Darwish, Saqer
Journal Title
Journal ISSN
Volume Title
Publisher
BioMed Central
Abstract
The interaction of Human Serum Albumin (HSA) with local
anaesthetic, procaine hydrochloride is an important study
from the viewpoint of pharmaceutical sciences to clarify the
structure, function, and properties of HSA-drug complexes.
The investigation has been carried through UV-absorption,
Fluorescence and FTIR spectroscopy. The secondary
structure of the protein and the binding mechanisms of the
drug have been studied using Fourier self-deconvolution
techniques on the obtained IR spectra.
Analysis of UV-absorbance and fluorescence spectra of
procaine-HSA complexes showed a weak binding ability in
quenching the intrinsic fluorescence of HSA by
combinations of static and dynamic quenching procedures.
The binding constant (k) is calculated by graphical analysis
and found to be in the range of (1.115-1.156) × 103 M-1 at
293 K. Spectral analysis of HSA-procaine compound has
revealed a relative decrease in the intensity of the
absorption band of α helix relative to that of β-sheets. This
change in intensity is mainly due to the formation of Hbonding
in procaine-HSA complex.
Keywords: Procaine; HSA; Binding constant; Protein
secondary structure; FT-IR spectroscopy
Description
Keywords
Citation
Alsamamra H, Khalid I, Alfaqeh R, Farroun M, Abuteir M, et al. (2018) Spectroscopic investigation of Procaine Interaction with Human Serum Albumin. J Biomedical Sci Vol.7 No.3:8.