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

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 pi-alkyl interaction. The co-oligomers showed high binding affinity toward HSA as compared to BSA which could be utilized for developing protein sensors.

Automated summary

Water-soluble polyfuran and polythiophene co-oligomers were synthesized and their biophysical interactions with bovine serum albumin and human serum albumin were studied. The interactions were found to be higher with human serum albumin, and were mediated through hydrogen bonding and pi-alkyl interaction. These co-oligomers showed high binding affinity towards human serum albumin, suggesting their potential use in protein sensors.