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@article{Pérez:2026:10.1002/anie.202513289,
author = {Pérez, LR and King, TA and Finnigan, W and Angelastro, A and Cain, KM and Eldrid-Otterburn, C and Houghton, JW and Tate, EW and Barran, P and Goundry, WRF and Flitsch, SL},
doi = {10.1002/anie.202513289},
journal = {Angew Chem Int Ed Engl},
title = {Selective N-Terminal Modification of Peptides and Proteins Using Fatty Acyl Phosphates.},
url = {http://dx.doi.org/10.1002/anie.202513289},
volume = {65},
year = {2026}
}
TY - JOUR
AB - The selective modification of proteins and peptides is an important chemical biology tool with a wide variety of applications, including the production of biopharmaceuticals or the study of post-translational modifications. In particular, the selective acylation of the N-terminus over side chains in peptides and proteins is a highly desirable but challenging reaction in this field. Current methods have a range of shortcomings, including lack of selectivity or narrow substrate scope. Here we report a biomimetic approach using the in situ enzymatic reagent activation (ERA) of carboxylic acids with ATP to generate acyl-adenosine monophosphates. This method displays high selectivity for the N-termini of peptides and proteins, including pharmaceutically relevant liraglutide, glucagon and insulin. The ERA acylation tolerates a broad range of unsubstituted and substituted fatty acids, including azido and dicarboxylic acids, thus making it suitable for N-terminal bioorthogonal labelling strategies. Moreover, this strategy can also be applied to the modification of antibodies. In general, the ERA acylation is a versatile and bioorthogonal method that we envisage finding wider applications in the field of bioconjugation and the production of stable peptide and protein conjugates.
AU - Pérez,LR
AU - King,TA
AU - Finnigan,W
AU - Angelastro,A
AU - Cain,KM
AU - Eldrid-Otterburn,C
AU - Houghton,JW
AU - Tate,EW
AU - Barran,P
AU - Goundry,WRF
AU - Flitsch,SL
DO - 10.1002/anie.202513289
PY - 2026///
TI - Selective N-Terminal Modification of Peptides and Proteins Using Fatty Acyl Phosphates.
T2 - Angew Chem Int Ed Engl
UR - http://dx.doi.org/10.1002/anie.202513289
UR - https://www.ncbi.nlm.nih.gov/pubmed/41510599
VL - 65
ER -
Prof. Ed Tate
GSK Chair in Chemical Biology
Department of Chemistry
Molecular Sciences Research Hub, White City Campus,
82 Wood Lane, London, W12 0BZ
e.tate@imperial.ac.uk
Tel: +44 (0)20 759 + ext 43752 or 45821