The next scientists presenting will be Dr Mohamed Elsawy from the University of Manchester and Prof Jamie Baker from University College London.
Date: 05-09-2025
Time: 1:00-2:00 pm
Venue: an online Zoom seminar
Registration link: https://eu01web.zoom.us/meeting/register/MlLWdc8jQIS1FXa9MJHxUg
Dr Mohamed Elsawy
Lecturer in Pharmaceutical Sciences, University of Manchester
鈥淎ssembling peptides: A chemical toolbox for the design of antimicrobial nanomaterials鈥�
The molecular engineering of bioinspired assembling peptides has been widely studied in the last two decades for the development of functional biomaterials [1]. In this context, our research focus on the rational design of libraries of assembling peptides, in which we consider and manipulate a variety of non-covalent interactions, to govern the thermodynamic stability and morphology of the resulting supramolecular nano-assemblies. In this talk, we will focus on how aromatic stacking, charge distribution and complementarity govern peptide 尾-sheet formation and lateral association, consequently affecting both nanofibre morphology and the mechanical properties of the resulting hydrogels [2,3]. We will also shed the light on how the nanoscopic properties of peptide hydrogels could affect their antibacterial and anti-biofilm activities against a range of pathogenic bacteria, the ESKAPE pathogens, which are commonly involved in topical and wound infections and possess multi-drug resistance against various antibiotics. This is a promising strategy for combating antimicrobial resistance in infected wounds, via utilising rationally designed peptide nanofibres that are capable of disrupting bacterial membranes.
[1] Elsawy M. (Editor), Peptide Bionanomaterials: From Design to Application. Springer, Cham. 2023 (ISBN 978-3-031-29360-3)
[2] Soliman M. et al., Small 2025; 2408213 (DOI: 10.1002/smll.202408213)
[3] Wychowaniec J. et al., Biomacromolecules 2020; 2670 (DOI: 10.1021/acs.biomac.0c00366)
Prof Jamie Baker
Professor of Chemistry, University College London
Title: "Biocompatible dithiol selective chemistries and their application to antibody conjugates as targeted therapeutics"
Abstract: Selective labelling of thiols - particularly cysteine residues in peptides and proteins - is a cornerstone technique in chemical biology and related disciplines. Such methods enable the precise construction of bioconjugates, yielding well-defined constructs that support a broad range of biological investigations and therapeutic applications. However, in many peptides and proteins, free cysteine residues are unavailable, instead existing in the form of disulfide bonds. Reduction of these disulfides to dithiols presents an opportunity to exploit them through a novel bioconjugation strategy known as disulfide re-bridging. This presentation will briefly describe several reagent classes we have developed to achieve highly efficient disulfide re-bridging, before discussing their application in the development of diverse antibody conjugates. Such conjugates combine the precise targeting capabilities of antibodies with the versatile functionality of small molecules, forming the foundation of numerous therapeutic and diagnostic platforms. Attention will then shift to discussing ongoing investigations into dithiol-selective chemistries, including the nitrile鈥揵isthiol (NBT) reaction as a new bioorthogonal methodology.
Date: 05-09-2025
Time: 1:00-2:00 pm
Venue: an online Zoom seminar
Registration link: https://eu01web.zoom.us/meeting/register/MlLWdc8jQIS1FXa9MJHxUg
Dr Mohamed Elsawy
Lecturer in Pharmaceutical Sciences, University of Manchester
鈥淎ssembling peptides: A chemical toolbox for the design of antimicrobial nanomaterials鈥�
The molecular engineering of bioinspired assembling peptides has been widely studied in the last two decades for the development of functional biomaterials [1]. In this context, our research focus on the rational design of libraries of assembling peptides, in which we consider and manipulate a variety of non-covalent interactions, to govern the thermodynamic stability and morphology of the resulting supramolecular nano-assemblies. In this talk, we will focus on how aromatic stacking, charge distribution and complementarity govern peptide 尾-sheet formation and lateral association, consequently affecting both nanofibre morphology and the mechanical properties of the resulting hydrogels [2,3]. We will also shed the light on how the nanoscopic properties of peptide hydrogels could affect their antibacterial and anti-biofilm activities against a range of pathogenic bacteria, the ESKAPE pathogens, which are commonly involved in topical and wound infections and possess multi-drug resistance against various antibiotics. This is a promising strategy for combating antimicrobial resistance in infected wounds, via utilising rationally designed peptide nanofibres that are capable of disrupting bacterial membranes.
[1] Elsawy M. (Editor), Peptide Bionanomaterials: From Design to Application. Springer, Cham. 2023 (ISBN 978-3-031-29360-3)
[2] Soliman M. et al., Small 2025; 2408213 (DOI: 10.1002/smll.202408213)
[3] Wychowaniec J. et al., Biomacromolecules 2020; 2670 (DOI: 10.1021/acs.biomac.0c00366)
Prof Jamie Baker
Professor of Chemistry, University College London
Title: "Biocompatible dithiol selective chemistries and their application to antibody conjugates as targeted therapeutics"
Abstract: Selective labelling of thiols - particularly cysteine residues in peptides and proteins - is a cornerstone technique in chemical biology and related disciplines. Such methods enable the precise construction of bioconjugates, yielding well-defined constructs that support a broad range of biological investigations and therapeutic applications. However, in many peptides and proteins, free cysteine residues are unavailable, instead existing in the form of disulfide bonds. Reduction of these disulfides to dithiols presents an opportunity to exploit them through a novel bioconjugation strategy known as disulfide re-bridging. This presentation will briefly describe several reagent classes we have developed to achieve highly efficient disulfide re-bridging, before discussing their application in the development of diverse antibody conjugates. Such conjugates combine the precise targeting capabilities of antibodies with the versatile functionality of small molecules, forming the foundation of numerous therapeutic and diagnostic platforms. Attention will then shift to discussing ongoing investigations into dithiol-selective chemistries, including the nitrile鈥揵isthiol (NBT) reaction as a new bioorthogonal methodology.
