Mechanistic insight into light-driven site-selective modification of proteins Ajay Jha 1,2, Xiaping Fu 1 , Carla Walla 3 , Greg Greetham 4 and Benjamin G. Davis 1,2,3 1 Rosalind Franklin Institute, Harwell, Oxfordshire, OX11 0QX, UK, 2 Department of Pharmacology, University of Oxford, Oxford, OX1 3QT, UK, 3 Department of Chemistry, University of Oxford, Oxford, OX1 3TA, UK, 4 STFC Central Laser Facility, Rutherford Appleton Laboratory, Harwell Campus, Didcot, OX11 0QX, UK Traditional methods of protein modification frequently use side chain bonds to heteroatoms (non-carbon) at the γ or ω locations. However, the rare but potentially significant divergence between synthetic and chemical life is the construction of C β -X bonds via C β , which is present in all amino acid side chains. We have been pursuing the use of light induced homolytic chemistries that can be combined with easily produced dehydroalanine residues on peptides/proteins. 1,2 Here, mechanistic insight into these photoinduced reactions using the transient absorption spectroscopic measurements within UV/Vis and mid-IR probe frequency windows will be presented. Additionally, an important role of charge transfer states in achieving higher product yields will also be discussed. References 1. Josephson et al., Nature 585, 530-537 (2020). 2. Fu et al. , biorxiv(2022) www.biorxiv.org/content/10.1101/2022.08.22.504816v1
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