Poster Title

Exploiting the reactivity of sortase homologs for generating isopeptide bonds

Research Mentor(s)

John Antos

Affiliated Department

Chemistry

Sort Order

25

Start Date

17-5-2017 12:00 PM

End Date

17-5-2017 3:00 PM

Document Type

Event

Abstract

Chemically modified proteins are becoming increasingly attractive for their utility in medicine and basic research. A challenge for organic chemists is precise and reproducible manipulation of proteins that result in new function. Sortase enzymes are able to generate protein conjugates such as antibody derivatives, modified viral particles, and multiprotein fusions. To expand on these capabilities, we are working to exploit the reactivity of sortase homologs for generating isopeptide bonds. Exploration of sortase A from S.suis, S. oralis, and S. pneumoniae is underway with the goal of using the transacylation activity of these enzymes for controlled modification of lysine residues in vitro. Optimization of model ligation reactions will be presented, as well as structure function studies related to the structure of suitable lysine-containing reaction components.

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 documentation 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 17th, 12:00 PM May 17th, 3:00 PM

Exploiting the reactivity of sortase homologs for generating isopeptide bonds

Chemistry

Chemically modified proteins are becoming increasingly attractive for their utility in medicine and basic research. A challenge for organic chemists is precise and reproducible manipulation of proteins that result in new function. Sortase enzymes are able to generate protein conjugates such as antibody derivatives, modified viral particles, and multiprotein fusions. To expand on these capabilities, we are working to exploit the reactivity of sortase homologs for generating isopeptide bonds. Exploration of sortase A from S.suis, S. oralis, and S. pneumoniae is underway with the goal of using the transacylation activity of these enzymes for controlled modification of lysine residues in vitro. Optimization of model ligation reactions will be presented, as well as structure function studies related to the structure of suitable lysine-containing reaction components.