Rate constants and dissociation constants of the interactions of scFv-IC16 and IC16 with N-terminal Aβ fragments.

Data were fitted globally. scFv-IC16 data were fitted according to the Langmuir 1∶1 binding model, whereas IC16 data were fitted using a bivalent fit. The association rate constants (kon), the dissociation rate constants (koff) and the equilibrium dissociation constants (KD) are given below. Both, scFv-IC16 and IC16, did not show any detectable binding towards Aβ(8-15). However, they showed binding to all N-terminal peptides, except scFv-IC16 did not bind to Aβ(pE3-8). The lowest KD value was observed for the interaction of scFv-IC16 and IC16 to Aβ(2-8).