Format

Send to

Choose Destination
Protein Eng Des Sel. 2013 Oct;26(10):683-93. doi: 10.1093/protein/gzt037. Epub 2013 Aug 21.

Two ScFv antibody libraries derived from identical VL-VH framework with different binding site designs display distinct binding profiles.

Author information

1
Department of Biochemistry and Food Chemistry, University of Turku, 20520 Turku, Finland.

Abstract

In directed evolution experiments, a single randomization scheme of an antibody gene does not provide optimal diversity for recognition of all sizes of antigens. In this study, we have expanded the recognition potential of our universal library, termed ScFvP, with a second distinct diversification scheme. In the second library, termed ScFvM, diversity was designed closer to the center of the antigen binding site in the same antibody framework as earlier. Also, the CDR-H3 loop structures were redesigned to be shorter, 5-12 aa and mostly without the canonical salt bridge between Arg106H and Asp116H to increase the flexibility of the loop and to allow more space in the center of the paratope for binding smaller targets. Antibodies were selected from the two libraries against various antigens separately and as a mixture. The origin and characteristics of the retrieved antibodies indicate that complementary diversity results in complementary functionality widening the spectrum of targets amenable for selection.

KEYWORDS:

CDR-H3; antibody library; phage display; single framework; synthetic diversity

PMID:
23966567
DOI:
10.1093/protein/gzt037
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Silverchair Information Systems
Loading ...
Support Center