Synthetic organic approaches for the covalent inhibition of protein-protein interactions
Synthetic organic approaches for the covalent inhibition of protein-protein interactions
This thesis described the design and synthesis of non-peptidic scaffolds that mimic secondary protein structure, with the aim of developing potent and selective proof-of-principle protein-protein interaction (PPI) inhibitors. The scaffolds consisted of conformationally preorganised ⍺-helical or βsheet mimetics, with a boron-centred electrophilic warhead which can form reversible covalent interactions with N- or O-centred Lewis basic/nucleophilic amino acid residues at a protein binding interface
University of Southampton
Bavinton, Clementine Ella
7fb75a01-95f8-4eeb-8c1b-0d566c0d71be
September 2022
Bavinton, Clementine Ella
7fb75a01-95f8-4eeb-8c1b-0d566c0d71be
Thompson, Sam
99b7e34e-fe24-401c-b7b0-64e56cbbbcb1
Bavinton, Clementine Ella
(2022)
Synthetic organic approaches for the covalent inhibition of protein-protein interactions.
University of Southampton, Doctoral Thesis, 270pp.
Record type:
Thesis
(Doctoral)
Abstract
This thesis described the design and synthesis of non-peptidic scaffolds that mimic secondary protein structure, with the aim of developing potent and selective proof-of-principle protein-protein interaction (PPI) inhibitors. The scaffolds consisted of conformationally preorganised ⍺-helical or βsheet mimetics, with a boron-centred electrophilic warhead which can form reversible covalent interactions with N- or O-centred Lewis basic/nucleophilic amino acid residues at a protein binding interface
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Published date: September 2022
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Local EPrints ID: 473113
URI: http://eprints.soton.ac.uk/id/eprint/473113
PURE UUID: 71ac77dd-20f8-4388-99b6-151f1620262b
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Date deposited: 10 Jan 2023 18:17
Last modified: 17 Mar 2024 03:41
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Author:
Clementine Ella Bavinton
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