The role of an enzyme highly relies on the structure and conformation which is mainly characterized by the secondary conformation of peptide backbone. The assembly of an artificial material with secondary structure through a specific path has been a challenging problem. Biomimetic, graphene oxide (GO) can be used as an artificial receptor for molecular recognition study. The dual physical properties (electrostatic vs. hydrophobic) of GOs present if different facet which can be used as site-specific interactions to generate protein mimicking artificial systems. In this regard, we have designed three different peptides which consist specific recognizer amino acid residue at specific interim i.e., arginine (peptide 1) and aspartic acid (peptide 2) introduced for electrostatic interaction and tryptophan (peptide 3) for hydrophobic interactivity. To examine the effect of GO on secondary structure of peptides, we have incubated those peptides with GO and monitor their secondary structure by Circular Dichroism study. In the presence of GO, peptide1 and peptide 3 acquire a-helical conformation in contrast to the initial random coil state. But peptide 2 does not show any such change. This indicates the peptide can bind to GO through site-specifically and initiate the secondary conformation. Additionally, the interaction can be controlled from edge to surface of 2D materials depending on peptide design.

Biomimetic 2D template graphene oxide: A potential candidate to induced super α-helices orientation from random coils peptides

ACS Spring Meeting 2021

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.