Abstract
Binding of farrerol to lysozyme (LYSO) was investigated at 302, 313 and 318 K at pH 7.4 using spectrophotometric techniques such as fluorescence emission, circular dichroism (CD) and UV absorption. The data obtained from fluorescence quenching experiments showed that farrerol was bound to LYSO and the affinity was enhanced by the addition of farrerol. When the concentration ratio of farrerol to LYSO was higher than 5.4, both the binding constant and the binding stoichiometry went up. Based on the thermodynamic parameters evaluated from the van’t Hoff equation, the enthalpy change (Δ H°) and entropy change (Δ S°) were derived to be negative values. They indicated that both van der Waals forces and hydrogen bonds are the major interactions between farrerol and LYSO. A value of 2.67 nm for the average distance r between farrerol (acceptor) and tryptophan residues (Trp) of LYSO (donor) was derived from the fluorescence resonance energy transfer. Besides, the change in the conformation of LYSO was observed, being caused by the interaction with farrerol.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
