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Title: Methods and compositions to increase the rate of ligation reactions catalyzed by a sortase

Abstract

In various embodiments methods and compositions to increase the rate and/or activity of ligation reactions catalyzed by a sortase. In certain embodiments reagents are provided that comprises, inter alia, a polypeptide comprising an amino terminal polyglycine sequence comprising at least three contiguous Gly residues (e.g., a triglycine sequence, a tetraglycine sequence, a pentaglycine sequence, etc.) followed by a peptide that is to be ligated to a moiety followed by a sequence comprising the catalytic domain of a Sortase A enzyme.

Inventors:
;
Issue Date:
Research Org.:
Univ. of California, Oakland, CA (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Biological and Environmental Research (BER)
OSTI Identifier:
1735224
Patent Number(s):
10766923
Application Number:
16/072,155
Assignee:
The Regents of the University of California (Oakland, CA)
Patent Classifications (CPCs):
C - CHEMISTRY C07 - ORGANIC CHEMISTRY C07K - PEPTIDES
C - CHEMISTRY C12 - BIOCHEMISTRY C12N - MICROORGANISMS OR ENZYMES
DOE Contract Number:  
FC02-02ER63421
Resource Type:
Patent
Resource Relation:
Patent File Date: 01/26/2017
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY

Citation Formats

Clubb, Robert T., and Amer, Brendan R. Methods and compositions to increase the rate of ligation reactions catalyzed by a sortase. United States: N. p., 2020. Web.
Clubb, Robert T., & Amer, Brendan R. Methods and compositions to increase the rate of ligation reactions catalyzed by a sortase. United States.
Clubb, Robert T., and Amer, Brendan R. Tue . "Methods and compositions to increase the rate of ligation reactions catalyzed by a sortase". United States. https://www.osti.gov/servlets/purl/1735224.
@article{osti_1735224,
title = {Methods and compositions to increase the rate of ligation reactions catalyzed by a sortase},
author = {Clubb, Robert T. and Amer, Brendan R.},
abstractNote = {In various embodiments methods and compositions to increase the rate and/or activity of ligation reactions catalyzed by a sortase. In certain embodiments reagents are provided that comprises, inter alia, a polypeptide comprising an amino terminal polyglycine sequence comprising at least three contiguous Gly residues (e.g., a triglycine sequence, a tetraglycine sequence, a pentaglycine sequence, etc.) followed by a peptide that is to be ligated to a moiety followed by a sequence comprising the catalytic domain of a Sortase A enzyme.},
doi = {},
journal = {},
number = ,
volume = ,
place = {United States},
year = {Tue Sep 08 00:00:00 EDT 2020},
month = {Tue Sep 08 00:00:00 EDT 2020}
}

Works referenced in this record:

Sortase A as a Novel Molecular “Stapler” for Sequence-Specific Protein Conjugation
journal, March 2007


Enzyme-Mediated Site-Specific Antibody−Protein Modification Using a ZZ Domain as a Linker
journal, December 2010


Attachment of an NMR-invisible solubility enhancement tag using a sortase-mediated protein ligation method
journal, January 2009


Rapid addition of unlabeled silent solubility tags to proteins using a new substrate-fused sortase reagent
journal, February 2016


Lipid Modification of Proteins through Sortase-Catalyzed Transpeptidation
journal, December 2008


Observing selected domains in multi-domain proteins via sortase-mediated ligation and NMR spectroscopy
journal, December 2010


Multi component antibody based detection technology
patent, March 2017


Synthesis of Biologically Active Peptide Nucleic Acid−Peptide Conjugates by Sortase-Mediated Ligation
journal, May 2007


Sortase enzymes in Gram-positive bacteria: Sortase enzymes in Gram-positive bacteria
journal, November 2011


Protein-Protein Fusion Catalyzed by Sortase A
journal, April 2011


Efficient segmental isotope labeling of multi-domain proteins using Sortase A
journal, August 2015


Covalent Attachment of Proteins to Solid Supports and Surfaces via Sortase-Mediated Ligation
journal, November 2007


Versatile Recombinant SUMOylation System for the Production of SUMO-Modified Protein
journal, July 2014