Investigating of cyanidin binding behavior upon interaction with human serum albumin and human transferrin: biophysical and molecular docking approaches

Introduction: Cyanidin, a compound found in fruits, is the derivative from flavonoid. due to its antioxidant property, cyanidin help prevent a variety of fee oxygen radical related diseases, including cancer, diabetes, asthma and cardiovascular. Human serum albumin is the most abundant protein in the circulation system. Human transferrin is responsible for both exogenous and endogenous substance and donates iron to cells through interaction with a specific membrane receptor. The aims of this study is how cyanidin affected HSA and HTF by using biophysical methods.Materials and methods: The fluorescence measurements can provide some information about the binding constant, binding mechanism of drug protein interaction. RLS has been utilize to study of the shape, size and aggregation of biological and chemical species. Molecular docking was performed to predict the binding site location of CYA on HSA and HTF.Result and discussion: The fluorescence emission intensity of HSA and HTF reduced gradually upon interaction with cyanidin. This quenching induces information about complex forming and drug binding interaction. The RLS intensities of HSA_CYA and HTF _CYA increased with the increasing the concentration of the drug concentration. it can be deuced that the occurrence of an interaction between CYA and proteins has led to production of larger particles and consequently enhanced the RLS signals. The best molecular docking results for both HSA and HTF demonstrated that the 425GLU and 109ASN of HSA interacted with cyanidin through hydrogen bonds and 15GLU ,292ASP, 124ARG and 189SER of HTF were the most sensitive residue in this interface.Conclusion: In this study we determined the binding behavior of cyanidin upon interaction with HSA and HTF by using the biophysical methods and molecular docking. The calculated binding mechanism suggests a stable and possibly biologically relevant interaction.

کلیدواژه ها:

Cyanidin ، Human serum albumin ، Human transferrin ، Spectroscopy ، molecular docking