Kinetics of interaction between 3-hydroxyphthaloyl-beta-lactoglobulin and CD4 molecules.
Kinetics of 3-hydroxyphthaloyl-beta-lactoglobulin-CD4 interaction were evaluated using a biosensor instrument based on surface plasmon resonance. A very fast association (k(a)=2.4+/-0.3x10(6)M(-1)s(-1)) and slow dissociation (K(d)=2.3+/-0.14x10(-4)s(-1)) rate constants were observed indicating the high affinity of the complex. This result together with earlier data, suggest that "structure-specific" requirements must be met to endow acid anhydride modified lactoglobulin with the capacity for high affinity binding to CD4.
Zeder-Lutz
G
G
UPR 9021-Immunochimie des Peptides et des Virus., Institut de Biologie Moléculaire et Cellulaire du CNRS 15 rue René Descartes., 67084 Strasbourg Cedex, France.
Neurath
A R
AR
Van Regenmortel
M H
MH
D000818:Animals; D000998:Antiviral Agents / Q000378:metabolism* / Q000494:pharmacology; D001667:Binding, Competitive / Q000187:drug effects; D015374:Biosensing Techniques; D015704:CD4 Antigens / Q000378:metabolism*; D002417:Cattle; D004305:Dose-Response Relationship, Drug; D007700:Kinetics; D007782:Lactoglobulins / Q000378:metabolism* / Q000494:pharmacology; D013997:Time Factors
C098082:3-hydroxyphthalic-beta-lactoglobulin; D000998:Antiviral Agents; D015704:CD4 Antigens; D007782:Lactoglobulins