Generation of Proteins with Free N-Terminal Cysteine by Aminopeptidases.


Journal

Journal of the American Chemical Society
ISSN: 1520-5126
Titre abrégé: J Am Chem Soc
Pays: United States
ID NLM: 7503056

Informations de publication

Date de publication:
30 11 2022
Historique:
pubmed: 16 11 2022
medline: 2 12 2022
entrez: 15 11 2022
Statut: ppublish

Résumé

Efficient, site-specific, and bio-orthogonal conjugation of chemical functionalities to proteins is of great utility in fundamental research as well as industrial processes (e.g., the production of antibody-drug conjugates and immobilization of enzymes for biocatalysis). A popular approach involves reacting a free N-terminal cysteine with a variety of electrophilic reagents. However, current methods for generating proteins with N-terminal cysteines have significant limitations. Herein we report a novel, efficient, and convenient method for producing recombinant proteins with free N-terminal cysteines by genetically fusing a Met-Pro-Cys sequence to the N-terminus of a protein of interest and subjecting the recombinant protein to the sequential action of methionine and proline aminopeptidases. The resulting protein was site-specifically labeled at the N-terminus with fluorescein and a cyclic cell-penetrating peptide through native chemical ligation and a 2-cyanobenzothiazole moiety, respectively. In addition, the optimal recognition sequence of

Identifiants

pubmed: 36378906
doi: 10.1021/jacs.2c10194
pmc: PMC9923720
mid: NIHMS1870897
doi:

Substances chimiques

Cysteine K848JZ4886
Aminopeptidases EC 3.4.11.-
Recombinant Proteins 0
Fluorescein TPY09G7XIR
Peptide Library 0

Types de publication

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

Langues

eng

Sous-ensembles de citation

IM

Pagination

21763-21771

Subventions

Organisme : NCI NIH HHS
ID : P30 CA016058
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM110406
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM122459
Pays : United States
Organisme : NIH HHS
ID : S10 OD018507
Pays : United States

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Auteurs

Jordan P Hempfling (JP)

Ohio State Biochemistry Program, The Ohio State University, Columbus, Ohio 43210, United States.

Emily R Sekera (ER)

Department of Chemistry and Biochemistry, The Ohio State University, 484 West 12th Avenue, Columbus, Ohio 43210, United States.

Amar Sarkar (A)

Department of Chemistry and Biochemistry, The Ohio State University, 484 West 12th Avenue, Columbus, Ohio 43210, United States.

Amanda B Hummon (AB)

Ohio State Biochemistry Program, The Ohio State University, Columbus, Ohio 43210, United States.
Department of Chemistry and Biochemistry, The Ohio State University, 484 West 12th Avenue, Columbus, Ohio 43210, United States.
Comprehensive Cancer Center, The Ohio State University, Columbus, Ohio 43210, United States.

Dehua Pei (D)

Ohio State Biochemistry Program, The Ohio State University, Columbus, Ohio 43210, United States.
Department of Chemistry and Biochemistry, The Ohio State University, 484 West 12th Avenue, Columbus, Ohio 43210, United States.

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Classifications MeSH