Event Title

Exploiting the Reactivity of Sortase Homologs for Generating Isopeptide Bonds

Co-Author(s)

Sarah Bowersox

Research Mentor(s)

John Antos

Description

Chemically modified proteins are critical components of modern therapeutics and basic research. In order to access these materials, precise and reproducible methods for the manipulation of protein structure and properties are required. With this need in mind, sortase enzymes have risen to prominence due to their ability to catalyze highly selective ligations between protein targets and useful functional groups not typically encountered in nature. To expand on these capabilities, we are working to exploit the reactivity of sortase homologs for generating isopeptide bonds. Sortase analogs from S. suis were found to preferentially form isopeptide linkages in vitro, as confirmed by LC-MS and HPLC analysis. Optimization of model reactions will be presented as well as progress toward determining the optimal structure of suitable lysine-containing reaction components. Additionally, we will be discussing recent work using Ni(II) coordination to sequester reaction by-products and to push the reaction equilibrium towards products.

Document Type

Event

Start Date

16-5-2018 9:00 AM

End Date

16-5-2018 12:00 PM

Department

Chemistry

Comments

Outstanding Poster Award Recipient

Rights

Copying of this document in whole or in part is allowable only for scholarly purposes. It is understood, however, that any copying or publication of this document for commercial purposes, or for financial gain, shall not be allowed without the author’s written permission.

Language

English

Format

application/pdf

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May 16th, 9:00 AM May 16th, 12:00 PM

Exploiting the Reactivity of Sortase Homologs for Generating Isopeptide Bonds

Chemically modified proteins are critical components of modern therapeutics and basic research. In order to access these materials, precise and reproducible methods for the manipulation of protein structure and properties are required. With this need in mind, sortase enzymes have risen to prominence due to their ability to catalyze highly selective ligations between protein targets and useful functional groups not typically encountered in nature. To expand on these capabilities, we are working to exploit the reactivity of sortase homologs for generating isopeptide bonds. Sortase analogs from S. suis were found to preferentially form isopeptide linkages in vitro, as confirmed by LC-MS and HPLC analysis. Optimization of model reactions will be presented as well as progress toward determining the optimal structure of suitable lysine-containing reaction components. Additionally, we will be discussing recent work using Ni(II) coordination to sequester reaction by-products and to push the reaction equilibrium towards products.