The recognition of tetraaspartate peptide (2) by tetra-guanidinium (1) in (a) water and (b) aqueous methanol (10% H2O/90% CH3OH) has been investigated. The conformations of the free peptide and its complex with 1 have been characterized in both solvent systems by CD and 2D NMR spectroscopies. Increased α-helicity as a result of solvent composition and receptor binding are discussed. Control experiments show that the recognition stems from complementary electrostatic interactions, hydrogen bonding, and matching of surface topologies.
ASJC Scopus subject areas
- Colloid and Surface Chemistry