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Kinetic analysis of recombinant antibody-antigen interactions: Relation between structural domains and antigen binding

Kinetic analysis of recombinant antibody-antigen interactions: Relation between structural domains and antigen binding
Kinetic analysis of recombinant antibody-antigen interactions: Relation between structural domains and antigen binding

The relation between domain structures of recombinant monoclonal antibody fragments and their reaction kinetics was studied for the first time using a novel biosensor based on surface plasmon resonance technology. The association and dissociation rate constants of Fab, Fv and single domain (VH fragment) anti-lysozyme antibodies were determined and compared to the intact monoclonal antibody. Fab and Fv fragments showed similar reaction kinetics and had affinity constants of 6 X 109 M-1 and 25 X 109 M-1, respectively. The single domain antibody had significantly different reaction kinetics compared to the fragments consisting of paired heavy and light chain domains. The VH domain had both a higher dissociation and a lower association rate constant, which resulted in an affinity constant approximately 250 times lower than the Fab fragment. This rapid evaluation of antibody reaction kinetics should prove to be an important selection parameter when comparing antibody fragments for their utility in therapeutic or other applications.

1087-0156
Borrebaeck, Carl A. K.
37a90ec3-567a-4889-b084-da323cc44d47
Malmborg, Ann Christin
c0c07a5f-a194-4e33-938c-4382397cf11c
Furebring, Christina
279c34ef-c739-4de8-953f-ce53e9c3be72
Michaelsson, Anne
89421241-d342-4dc5-bbfa-470785fd6193
Ward, Sally
b31c0877-8abe-485f-b800-244a9d3cd6cc
Danielsson, Lena
80664773-cb30-4df2-a051-11c3c047ddc7
Ohlin, Mats
6f547303-0cf3-495b-b66c-7fb243c71c3d
Borrebaeck, Carl A. K.
37a90ec3-567a-4889-b084-da323cc44d47
Malmborg, Ann Christin
c0c07a5f-a194-4e33-938c-4382397cf11c
Furebring, Christina
279c34ef-c739-4de8-953f-ce53e9c3be72
Michaelsson, Anne
89421241-d342-4dc5-bbfa-470785fd6193
Ward, Sally
b31c0877-8abe-485f-b800-244a9d3cd6cc
Danielsson, Lena
80664773-cb30-4df2-a051-11c3c047ddc7
Ohlin, Mats
6f547303-0cf3-495b-b66c-7fb243c71c3d

Borrebaeck, Carl A. K., Malmborg, Ann Christin, Furebring, Christina, Michaelsson, Anne, Ward, Sally, Danielsson, Lena and Ohlin, Mats (1992) Kinetic analysis of recombinant antibody-antigen interactions: Relation between structural domains and antigen binding. Nature Biotechnology, 10 (6).

Record type: Article

Abstract

The relation between domain structures of recombinant monoclonal antibody fragments and their reaction kinetics was studied for the first time using a novel biosensor based on surface plasmon resonance technology. The association and dissociation rate constants of Fab, Fv and single domain (VH fragment) anti-lysozyme antibodies were determined and compared to the intact monoclonal antibody. Fab and Fv fragments showed similar reaction kinetics and had affinity constants of 6 X 109 M-1 and 25 X 109 M-1, respectively. The single domain antibody had significantly different reaction kinetics compared to the fragments consisting of paired heavy and light chain domains. The VH domain had both a higher dissociation and a lower association rate constant, which resulted in an affinity constant approximately 250 times lower than the Fab fragment. This rapid evaluation of antibody reaction kinetics should prove to be an important selection parameter when comparing antibody fragments for their utility in therapeutic or other applications.

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Published date: 1992

Identifiers

Local EPrints ID: 425259
URI: https://eprints.soton.ac.uk/id/eprint/425259
ISSN: 1087-0156
PURE UUID: c12f3ffa-41c9-4b78-bce6-951b7f16f48d
ORCID for Sally Ward: ORCID iD orcid.org/0000-0003-3232-7238

Catalogue record

Date deposited: 12 Oct 2018 16:30
Last modified: 14 Mar 2019 01:21

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Contributors

Author: Carl A. K. Borrebaeck
Author: Ann Christin Malmborg
Author: Christina Furebring
Author: Anne Michaelsson
Author: Sally Ward ORCID iD
Author: Lena Danielsson
Author: Mats Ohlin

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