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

Borrebaeck, Carl A K LU ; Malmborg Hager, Ann-Christin LU ; Furebring, Christina LU ; Michaelsson, Anne; Ward, Sally; Danielsson, Lena LU and Ohlin, Mats LU (1992) In Nature Biotechnology 10(6). p.697-698
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... (More)

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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Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
in
Nature Biotechnology
volume
10
issue
6
pages
697 - 698
publisher
Nature Publishing Group
external identifiers
  • Scopus:14744294558
ISSN
1087-0156
DOI
10.1038/nbt0692-697
language
English
LU publication?
yes
id
40caf4ce-2fdb-432f-b8a8-5c468b7fd44c
date added to LUP
2016-04-20 16:13:53
date last changed
2016-07-27 08:39:52
@misc{40caf4ce-2fdb-432f-b8a8-5c468b7fd44c,
  abstract     = {<p>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 10<sup>9</sup> M<sup>-1</sup> and 25 X 10<sup>9</sup> M<sup>-1</sup>, 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.</p>},
  author       = {Borrebaeck, Carl A K and Malmborg Hager, Ann-Christin and Furebring, Christina and Michaelsson, Anne and Ward, Sally and Danielsson, Lena and Ohlin, Mats},
  issn         = {1087-0156},
  language     = {eng},
  number       = {6},
  pages        = {697--698},
  publisher    = {ARRAY(0x84646d8)},
  series       = {Nature Biotechnology},
  title        = {Kinetic analysis of recombinant antibody-antigen interactions : Relation between structural domains and antigen binding},
  url          = {http://dx.doi.org/10.1038/nbt0692-697},
  volume       = {10},
  year         = {1992},
}