Affordable Access

Publisher Website

Dual surface selection methodology for the identification of thrombin binding epitopes from hotspot biased phage-display libraries

Authors
Journal
Bioorganic & Medicinal Chemistry Letters
0960-894X
Publisher
Elsevier
Publication Date
Volume
14
Issue
6
Identifiers
DOI: 10.1016/j.bmcl.2003.09.098
Disciplines
  • Biology

Abstract

Abstract Protein libraries biased towards amino-acid residues found at so-called ‘hotspots’ were incorporated into the beta-sheet region of the thermostable variant (HTB1) of the B1 domain of the immunoglobulin (IgG) binding protein G and expressed as gene 3 fusions on M13 bacteriophage. The HTB1 library (2.2×10 9) variants with a minimal 12 amino acid basis set were selected for binding IgG, to ensure structural conservation, and subsequently to thrombin to evolve a thrombin-binding function. We believe that this dual surface selection strategy will have great utility in evolving new bi-functional proteins without compromising structure. Furthermore the discrete beta-sheet epitopes identified by our methodology will lend itself to small-molecule mimicry of beta-sheets.

There are no comments yet on this publication. Be the first to share your thoughts.

Statistics

Seen <100 times
0 Comments

More articles like this

Dual surface selection methodology for the identif...

on Bioorganic & Medicinal Chemist... Mar 22, 2004

In vivo selection of sFv from phage display librar...

on Journal of Immunological Metho... May 26, 2000

In vivo selection of sFv from phage display librar...

on Journal of Immunological Metho... Jan 01, 2000

Phage display selection and analysis of Ab-binding...

on Current protocols in immunolog... November 2002
More articles like this..