Chemoselective restoration of para-azido-phenylalanine at multiple sites in proteins.

biomaterials click-chemistry conjugation genetic code expansion genomically recoded organisms non-standard amino acids para-azido-phenylalanine protein engineering

Journal

Cell chemical biology
ISSN: 2451-9448
Titre abrégé: Cell Chem Biol
Pays: United States
ID NLM: 101676030

Informations de publication

Date de publication:
16 06 2022
Historique:
received: 22 11 2020
revised: 02 06 2021
accepted: 30 11 2021
pubmed: 30 12 2021
medline: 22 6 2022
entrez: 29 12 2021
Statut: ppublish

Résumé

The site-specific incorporation of nonstandard amino acids (nsAAs) during translation has expanded the chemistry and function of proteins. The nsAA para-azido-phenylalanine (pAzF) encodes a biorthogonal chemical moiety that facilitates "click" reactions to attach diverse chemical groups for protein functionalization. However, the azide moiety is unstable in physiological conditions and is reduced to para-amino-phenylalanine (pAF). Azide reduction decreases the yield of pAzF residues in proteins to 50%-60% per azide and limits protein functionalization by click reactions. Here, we describe the use of a pH-tunable diazotransfer reaction that converts pAF to pAzF at >95% efficiency in proteins. The method selectively restores pAzF at multiple sites per protein without introducing off-target modifications. This work addresses a key limitation in the production of pAzF-containing proteins by restoring azides for multi-site functionalization with diverse chemical moieties, setting the stage for the production of genetically encoded biomaterials with broad applications in biotherapeutics, materials science, and biotechnology.

Identifiants

pubmed: 34965380
pii: S2451-9456(21)00516-X
doi: 10.1016/j.chembiol.2021.12.002
pmc: PMC10173106
mid: NIHMS1891803
pii:
doi:

Substances chimiques

Amino Acids 0
Azides 0
Biocompatible Materials 0
Proteins 0
Phenylalanine 47E5O17Y3R

Types de publication

Journal Article Research Support, Non-U.S. Gov't Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S.

Langues

eng

Sous-ensembles de citation

IM

Pagination

1046-1052.e4

Subventions

Organisme : NIGMS NIH HHS
ID : R01 GM125951
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM141192
Pays : United States

Informations de copyright

Copyright © 2021 Elsevier Ltd. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of interests The authors have filed a patent related to this work. F.J.I. is a co-founder of Pearl Bio.

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Auteurs

Pol Arranz-Gibert (P)

Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT, USA; Systems Biology Institute, Yale University, West Haven, CT, USA.

Koen Vanderschuren (K)

Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT, USA; Systems Biology Institute, Yale University, West Haven, CT, USA.

Adrian Haimovich (A)

Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT, USA; Systems Biology Institute, Yale University, West Haven, CT, USA.

Anushka Halder (A)

Department of Cell Biology, Yale University, New Haven, CT, USA; Nanobiology Institute, Yale University, West Haven, CT, USA.

Kallol Gupta (K)

Department of Cell Biology, Yale University, New Haven, CT, USA; Nanobiology Institute, Yale University, West Haven, CT, USA.

Jesse Rinehart (J)

Systems Biology Institute, Yale University, West Haven, CT, USA; Department of Cellular and Molecular Physiology, Yale University, New Haven, CT, USA.

Farren J Isaacs (FJ)

Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT, USA; Systems Biology Institute, Yale University, West Haven, CT, USA; Department of Biomedical Engineering, Yale University, New Haven, CT, USA. Electronic address: farren.isaacs@yale.edu.

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