Abstract:

Molecular self-assembly has been exploited in Nature to develop the complex higher macromolecular structures of both the genome and proteome. Our work focuses on understanding the fundamentals behind self-assembly of protein structures and learning lessons from those biomacromolecules for the design of de novo ultra-short, constrained peptides that self-assemble into bio-inspired fibril structures. Using chemical toolbox of amino acid building blocks, we adopt a bottom-up engineering approach for the rational design of our peptides, where the primary sequence dictates the resulting self-assembled nanostructure. We have manipulated those peptide-based nanostructures for the innovation of novel stable, responsive and functional bionanomaterials with various potential pharmaceutical, biomedical and biotechnological applications. Recently, we have started exploring the antimicrobial activity of our peptide nanofibrous hydrogels, in an attempt to overcome Antimicrobial Resistance (AMR) in infected wounds. 

AMR is one of the top public health challenges globally, estimated to have caused 4.95 million deaths in the last decade, of which 1.27 million reported in 2019. Innovative antimicrobial nanofibrous peptides could help minimise the reliance on antibiotics for the treatment of topical bacterial infections; an emerging strategy that could potentially contribute to overcoming AMR. 

In this context, we have investigated the antibacterial activity of our peptide β-sheet nanofibres against a range of pathogenic bacteria, the ESKAPE pathogens, which are commonly implicated in wound infections and possess multi-drug resistance against commonly used antibiotics. In essence, all tested nanofibres showed bactericidal activity against both Gram -ve and Gram +ve bacteria (including clinical isolates), as well as prevention of formation and disruption of biofilms. Electron microscopy revealed that the bactericidal activity is mediated via insertion of peptide nanofibres in the bacterial cell membrane, disrupting membrane integrity, which was confirmed by membrane staining assays. Cytocompatibility testing revealed the safety of the developed peptide nanofibres to mammalian cells (human dermal fibroblasts and RBCs) 

Our results suggest that applying our peptide nanofibres to chronic wound infections could help with treatment of infection and accelerate the healing process, where bacterial infection invading deeper layers of skin and causing significant tissue damage. 

About our speaker:

Dr Mohamed Elsawy is a Lecturer in Pharmaceutical Sciences at the University of Manchester (UK). He obtained his PhD from the School of Pharmacy at Queen’s University of Belfast (UK), funded by the John King Scholarship. His PhD focused on the rational design of helical peptides as pro-apoptotic agents for targeting protein-protein complexes within the BCl-2 family in cancer cells. 

After his PhD, he did a postdoctoral training at the Institut Européen de Chimie et Biologie at the University of Bordeaux (France) funded by the Campus France & at the Manchester Institute of Biotechnology, University of Manchester (UK) funded by the EPSRC. In 2017, he started the Peptide BioNanomaterials Group, where the research interest of his group focuses on understanding the fundamentals behind molecular self-assembly of peptides into bio-inspired nanostructures for the rational design of stable, responsive and functional novel bionanomaterials for pharmaceutical, biomedical and biotechnological applications. 

In 2026, he was awarded a Cross Research Council Responsive Mode (CRCRM) Grant, which is a major funding to launch a project on developing bioinspired peptide-based soft robots for precise regiospecific drug delivery to colorectal cancer. Dr Elsawy has authored over 54 peer-reviewed and conference publications, secured over £2.4 M from UKRI and Charities, mentored more than 23 early-career researchers (both PhDs and PDRAs), and plays an active leadership role in the international biomaterials community through the European Society of Biomaterials (ESB) and the Royal Society of Chemistry (RSC).