Faculty, Staff and Student Publications

Publication Date

1-1-2024

Journal

Methods in Molecular Biology

Abstract

Targeting dysregulated protease expression and/or abnormal substrate proteolysis, highly selective inhibition of pathogenic proteases by monoclonal antibodies (mAbs) presents an attractive therapeutic approach for the treatment of diseases including cancer. Herein, we report a functional selection method for protease inhibitory mAbs by periplasmic co-expression of three recombinant proteins-a protease of interest, an antibody Fab library, and a modified β-lactamase TEM-1. We validate this approach by isolation of highly selective and potent mAbs inhibiting human matrix metalloproteinase 9 (MMP9).

Keywords

Humans, Peptide Hydrolases, Matrix Metalloproteinase Inhibitors, Antibodies, Monoclonal, Endopeptidases, Proteolysis, : Inhibitory antibody, Functional selection, Matrix metalloproteinase

DOI

10.1007/978-1-0716-3589-6_19

PMID

38038945

PMCID

PMC10732120

PubMedCentral® Posted Date

1-1-2024

PubMedCentral® Full Text Version

Author MSS

Published Open-Access

yes

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