Using combinatorial methods to arrive at a quantitative structure–stability relationship for a new class of one-armed cationic peptide receptors targeting the C-terminus of the amyloid β-peptideElectronic supplementary information (ESI) available: quantitative on bead binding assay. See http://www.rsc.org/suppdata/ob/b2/b211425a/

Publisher Website
Google Scholar
Abstract
A new class of one-armed tripeptide based cationic guanidiniocarbonyl pyrrole receptors is shown to strongly bind the tetrapeptide L-Val-L-Val-L-Ile-L-Ala, representing the C-terminus of the amyloid β-peptide even under polar conditions. A medium sized combinatorial library of 125 receptors was synthesized on a solid support and their binding properties determined on bead using a quantitative fluorescence assay. The binding constants are in the order of 103–104 M−1 (in the presence of a formate counter ion in methanol) for the most efficient ones but differ by more than a factor of 100 among the 125 library members. Based on the binding data of 12 receptors a structure–stability relationship was established for peptide binding by this new receptor class. Complex formation is controlled by a fine balanced interplay of hydrophobic and electrostatic interactions with none of these two interactions alone being strong enough to ensure complexation under these polar conditions.

This publication has 0 references indexed in Scilit: