THE KINETICS AND AFFINITY OF BINDING OF GLU-PLASMINOGEN SPECIFIC TO THE EPSILON-AMINO GROUP OF L-LYSINE - ITS POTENTIAL APPLICATION TO MODIFIED BIOMATERIALS

By covalently coupling L-lysine to an analytical surface through a dip eptide linkage such that the epsilon-amino group is accessible, we hav e looked at plasminogen binding in real time. The results have led to a model of plasminogen interactions with epsilon-amino groups, This pa per focuses on the desorption kinetics of plasminogen adsorbed to this material, Plasminogen is shown to bind to the dipeptide in at least f our different ways to the epsilon-amino groups. It is suggested that s ome molecules bind to several epsilon-amino groups at the same time. T he surface plasmon resonance analysis also indicates that the interact ion of Glu-plasminogen with L-lysine is very complex and may not be de fined simply by discrete kringle interactions alone, Dissociation cons tants ranging from 0.1 s(-1) to less than 5 x 10(-7) s(-1) are observe d. This material may well represent a surface sufficiently similar as to mimic plasminogen binding to fibrin. (C) 1998 Academic Press.