My current research interests include the following:
Supramolecular Chemistry
Peptide Chemistry
Bio-nanotechnology
Functional Biomaterials
Hydrogels
Enzyme mimicry
Bio-nano catalysis
Drug Design and Therapeutics
Animal Diseases
Aim of Study:
Peptides can self-assemble into a variety of nanostructures, including nanofibrils, nanotubes, coiled-coil bundles, and micelles. These peptide-based supramolecular assemblies offer a unique platform for the self-assembly of catalytic residues and their spatial alignment, thereby enabling the development of bioinspired peptide-based catalysts for various chemical reactions. Peptides can be designed to mimic the active site of a natural enzyme by incorporating catalytic residues within the peptide sequence in a defined geometry that induces its catalytic performance. Different conformations of peptide-based architectures, including α-helical, β-sheet, and disordered, have been successfully designed to mediate various chemical transformations, such as hydrolysis, carbon-carbon bond formation, and aldol condensations. These peptide-based supramolecular systems provide a remarkable framework for designing catalysts, supporting both minimalist molecular constructs and more elaborate assemblies that emulate enzyme active sites. It underscores their potential as robust and adaptable platforms for sustainable chemical synthesis. Advancements in the field of peptide engineering and self-assembly provide a promising platform for the development of next-generation, tunable peptide-based materials for applications in diverse fields, including biocatalysis, environmental remediation, and biomedical engineering. We examined the rational feasibility of designing and functionalizing short peptides across four distinct research objectives. In the first objective, four sets of heterochiral heptapeptides were rationally designed to emulate the active site of the metalloenzyme human carbonic anhydrase II (hCAII). These peptides exhibited both esterase-like catalytic activity and hydration of carbon dioxide, enabling carbon dioxide sequestration at the laboratory scale and, hence, offering a promising step toward sustainable and environmentally friendly technologies. The second objective involved designing three Fmoc-protected tripeptides to mimic a hydrolase enzyme. These peptides demonstrated significant catalytic activity over a broad range of pH and temperature conditions, with findings highlighting that the positional variation of the histidine residue within the short peptide sequence profoundly influenced catalytic performance. The third objective addressed bioremediation applications, utilizing a short peptide-based hydrogel for the adsorption of toxic organic dyes. The hydrogel exhibited high dye removal efficiency, reusability, and biocompatibility, highlighting its potential as an environmentally safe remediation agent. Additionally, this peptide exhibited hydrolytic activity, capable of degrading di(2-ethylhexyl) phthalate (DEHP), a commonly used plasticizer, thereby demonstrating its utility in the environmental biodegradation of pollutants. In the final objective, the influence of external electric fields on peptide-based hydrogels was investigated. Electric field modulation significantly altered the properties of the peptide hydrogel, including morphology, conductivity, solubility, and mechanical properties. Notably, the enhanced solubility observed under specific field strengths suggests potential applications in therapeutic strategies for neurodegenerative diseases, including Alzheimer's disease.