November 2026 webinar on protein and peptide science
The next scientists presenting will be Dr Ewen Calder (University of Edinburgh) and Dr Seb Cosgrove (Keele University).
Date: 06-11-2026
Time: 1:00-2:00 pm
Venue: an online Zoom seminar
Dr Ewen Calder, University of Edinburgh
Title: Novel Flexizymes to Enable the Development of Fluorogenic Peptide Chemical Tools
Binding-activated sensors and imaging agents are powerful tools for microscopy, diagnostics and biomolecular interaction sensing.1 Recently, the development of peptide-based imaging tools and biosensors has been accelerated and streamlined through application of screening techniques such as mRNA display.2 However, many of these molecules are initially identified purely as binders of a target, necessitating their post-discovery functionalisation with fluorogenic or fluorescent groups. This frequently causes changes in the binding of molecules to their target, and can create new challenges in solubility or permeability. Direct incorporation of fluorogenic functional groups in the discovery phase, mitigates many of these challenges and can allow parallel in vitro development of novel sensors.3 Incorporation of these groups into mRNA display is possible by ribozyme-mediated (flexizyme) codon reprogramming, but only where tRNA charging is possible.4 While many noncanonical functional groups are tolerated by the current flexizymes (eFx, dFx and aFx) there are limited examples of incorporation of fluorogenic moieties. Here, I will discuss our development of a series of novel flexizymes which we have evolved to selectively load non-canonical nitrobenzoxadiazole-type (NBD) amino acids, our initial characterisation and validation of these and our work towards incorporation of these into the mRNA display peptide-screening platform we use.
[1] Wong, et al., Nat. Chem., 2026, DOI: 10.1038/s41557-026-02228-0.
[2] Cui, et al., ACS Sens., 2024, 9, 2846, DOI:10.1021/acssensors.3c02471.
[3] Kuru, et al., Nat Commun, 2024, 15, 7531, DOI: 10.1038/s41557-026-02228-0.
[4] Wu, et al., ChemMedChem, 2021, 16, 3185, DOI: 10.1002/cmdc.202100315.
Dr Sebastian Cosgrove, Keele University
Title: Enhancing oxidase enzymes through bioprocess optimisation: the need for better oxygen solutions
Oxidases are attractive oxidation catalysts that often require minimal cofactors and rely solely on atmospheric oxygen as the terminal oxidant. However, this apparent advantage presents a fundamental challenge: under atmospheric pressure, oxygen has a maximum solubility of around 8 mg L-1 (~0.27 mM) in aqueous solution. Many oxidases require higher oxygen concentrations for optimal activity, making oxygen availability a significant kinetic limitation under conventional reaction conditions. This talk will discuss factors governing oxygen binding in amine oxidases and describe the development of a reactor system designed to overcome oxygen mass transfer limitations. By increasing oxygen availability, this platform enabled substantially higher oxidase efficiencies than those achievable in standard batch processes. The reactor was subsequently integrated into a multi-stage continuous biocatalytic cascade, demonstrating the potential for process design to unlock the synthetic potential of oxidase enzymes and expand their application in chemical synthesis.
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