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

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Kinetic analysis of recombinant antibody-antigen interactions : Relation between structural domains and antigen binding. / Borrebaeck, Carl A K; Malmborg Hager, Ann-Christin; Furebring, Christina; Michaelsson, Anne; Ward, Sally; Danielsson, Lena; Ohlin, Mats.

In: Nature Biotechnology, Vol. 10, No. 6, 1992, p. 697-698.

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Borrebaeck, Carl A K ; Malmborg Hager, Ann-Christin ; Furebring, Christina ; Michaelsson, Anne ; Ward, Sally ; Danielsson, Lena ; Ohlin, Mats. / Kinetic analysis of recombinant antibody-antigen interactions : Relation between structural domains and antigen binding. In: Nature Biotechnology. 1992 ; Vol. 10, No. 6. pp. 697-698.

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TY - JOUR

T1 - Kinetic analysis of recombinant antibody-antigen interactions

T2 - Nature Biotechnology

AU - Borrebaeck, Carl A K

AU - Malmborg Hager, Ann-Christin

AU - Furebring, Christina

AU - Michaelsson, Anne

AU - Ward, Sally

AU - Danielsson, Lena

AU - Ohlin, Mats

PY - 1992

Y1 - 1992

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=14744294558&partnerID=8YFLogxK

U2 - 10.1038/nbt0692-697

DO - 10.1038/nbt0692-697

M3 - Article

VL - 10

SP - 697

EP - 698

JO - Nature Biotechnology

JF - Nature Biotechnology

SN - 1546-1696

IS - 6

ER -