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Lookup NU author(s): Professor Tiago OuteiroORCiD
This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License (CC BY-NC 4.0).
© 2024 The Author(s). ChemBioChem published by Wiley-VCH GmbH. The chemical rules governing protein folding have intrigued generations of researchers for decades. With the advent of artificial intelligence (AI), prediction of protein structure has improved tremendously. However, there is still a level of analysis that is only possible through wet laboratory experiments, especially in respect to the investigation of the pathological effect of mutations and posttranslational modifications (PTMs) on proteins of interest. This requires the availability of pure peptides and proteins in sufficient quantities for biophysical, biochemical, and functional studies. In this context, chemical protein synthesis and semi-synthesis are powerful tools in protein research, which help to enlighten the role of protein modification in the physiology and pathology of proteins. A protein of high interest in the field of biomedicine is alpha-synuclein (aSyn), a protein deeply associated with several devastating neurodegenerative disorders such as Parkinson's disease (PD), dementia with Lewy bodies (DLB), or multiple systems atrophy (MSA). Here, we describe several methods and pathways to synthesize native or modified aSyn, and discuss how these approaches enable us to address pathological mechanisms that may open novel perspectives for therapeutic intervention.
Author(s): Gatzemeier LM, Meyer F, Outeiro TF
Publication type: Article
Publication status: Published
Journal: ChemBioChem
Year: 2024
Volume: 25
Issue: 20
Print publication date: 16/10/2024
Online publication date: 23/08/2024
Acceptance date: 04/07/2024
Date deposited: 02/09/2024
ISSN (print): 1439-4227
ISSN (electronic): 1439-7633
Publisher: John Wiley and Sons Inc.
URL: https://doi.org/10.1002/cbic.202400253
DOI: 10.1002/cbic.202400253
PubMed id: 38965889
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