Molecular recognition forces , particularly hydrogen bonding interactions, are not only central to the structure formation of the biopolymers such as proteins, but also play pivotal role in the structural and functional property of synthetic polymers such as N-acrylamides. Acrylamides constitute a very important class of oligomers / polymers which find wide applications – for developing disposable nappies to microfluidic devices. Most of the "high-tech" applications make use of the specific property of reversible thermo-precipitation exhibited by certain types of acrylamide polymers. Intriguingly, till to date, the exact molecular mechanism of reversible thermo-precipitation is not known. We believe that unravelling this property that clearly involves diverse H-bonding interactions, would enormously help understand closely protein folding.

Extensive investigations from our group suggested that isotactic acrylamide oligomers assume sheet structures – reminiscent of protein beta sheets. Remarkably, there are distinctive differences between native protein sheets and the sheet structure assumed by isotactic acrylamide oligomers. Whereas the protein β-sheets make use of the hydrogen-bonding interactions from the backbone for molecular recognition events leading to self-assembly, the isotactic acrylamide oligomers utilize the amide groups of the side chain to attain self-assembled structural architecture. It is noteworthy that artificial strands could be very useful in biomedical science, since beta-strand is viewed as one of the fundamental structural elements that are specifically recognized by biomolecular receptors. Importantly, this work paves way for engineering novel artificial protein structures based on the acrylamide oligomer platform.

Prof. Samuel Gellman, University of Wisconsin - a pioneer in the field of Biopolymers, praised these findings (see the Chemical science magazine for a highlight of this work): In a post-publication review entitled "Polyacrylamide: 'It's not just for electrophoresis anymore.," Prof. Anthony Czarnik, University of Nevada, USA, a distinguished molecular biologist, rated this work as "exceptional".