Exploration of interaction existing between Methyl Chavicol and Bovine Serum Albumin using Spectroscopic and molecular modelling techniques

Abstract

Abstract Methyl Chavicol (MC), also known as 1-methoxy-4-prop-2-enylbenzene, estragole, or p-allyl anisole is a specific metabolite that can be found in the essential oils of both culinary and medicinal plants. It has anti-microbial, anti-inflammatory, and insecticidal properties. In order to determine the binding mechanism and conformational changes of the in vitro interaction of MC with bovine serum albumin (BSA), several biophysical techniques as well as molecular modelling methods have been used. The fluorescence emission from BSA in the presence of MC at three distinctive temperatures was measured using 290nm excitation wavelength. BSA's intrinsic fluorescence has been quenched by MC via a static process. The absorption peak shifts as a result of the development of the MC-BSA complex. Binding of MC with BSA caused conformational alterations, as seen by the fluorescence, UV- absorption, circular Dichroism, and FT-IR data. The values of the binding constants get increased as the temperature rises, indicating a stable complex formation under these conditions. Further, Site II, of BSA, has been discovered to have the strongest MC binding affinity and hydrophobic interactions have been hypothesized to be the dominant interaction type in the BSA-MC complex because of the positive levels of enthalpy and entropy changes.