Synthesis and characterization of polyfuran/polythiophene oligomers: Oligomer–protein interaction studies

Abstract

Water-soluble polyfuran (PF), polythiophene (PTh), and their co-oligomers were synthesized and the formation of the oligomers was confirmed by FTIR, UV–visible, and SEM techniques. Bovine serum albumin (BSA) and human serum albumin (HSA) were used to study the biophysical interaction of these oligomers with proteins. Molecular docking studies confirmed that the interaction with HSA was higher than that for BSA and was found be via hydrogen bonding and π-alkyl interaction. The co-oligomers showed high binding affinity toward HSA as compared to BSA which could be utilized for developing protein sensors.