Experimental and biophysical interaction studies of alanine modified polyaniline with bovine serum albumin and human serum albumin: Influence of alanine modification on the spectral, morphological and electronic properties

The present work reports for the first time, modification of aniline with alanine (Ala) in mole ratios of 80-20, 50-50 and 20-80 via ultrasound-assisted polymerization. The formation of Ala-incorporated polyaniline (PANI) was confirmed via FTIR, UV-visible and SEM studies. The geometry optimization, Mulliken charge distribution, vibrational as well as electronic spectral analysis was carried out using Gaussian 09 software with B3LYP/6311 G (d) basis set. Quenching of bovine serum albumin (BSA) and human serum albumin (HSA) by Ala/PANI followed the static mechanism which was confirmed by the fluorescence studies and Stern Volmer plots. The binding constant (Kb) values were found to be higher for Ala-PANI oligomers (similar to 105 LM 1) containing higher loading of PANI. The binding affinity of Ala/PANI towards BSA as well as HSA was found to be fairly good and the docking studies established that hydrogen bonding as well as Van der Waal's forces played a significant role in the binding process.

Automated summary

This study for the first time reports the modification of aniline with alanine using ultrasound-assisted polymerization. The formation of Ala-incorporated polyaniline (PANI) was confirmed by various analyses. The binding affinity of Ala/PANI towards BSA and HSA was found to be good, with hydrogen bonding and Van der Waal's forces playing a significant role.