Calix[8]arene‐mediated self‐assembly of tetrapeptide H‐Leu‐Leu‐Ile‐Leu‐OMe

Conformational analysis of peptide 1 , H‐Leu‐Leu‐Ile‐Leu‐OMe on complexing with macro cycle calix[8]arene has been carried out using 1 H‐NMR and FTIR spectroscopic techniques. Stoichiometry of the complex formed in the 1:8 ratio was evidenced by a Job plot. NMR studies of the above peptide show a marked downfield shift and an increase in 3 J values for NH resonances on complexing with calix[8]arene. The characteristic NOE connectivity between N i+1 H and C iα H confirm β‐sheet conformation in the complexed state. Both 1 H‐NMR and FTIR results indicate that the α‐amino group of Leu I is proximal to the macrocycle and is involved in hydrogen bond formation with phenolic hydrogen atom of the calix[8]arene. This suggests that calix[8]arene provides a suitable platform for peptide 1 to self‐assemble in a parallel β‐sheet conformation. The nature of calix[8]arene interaction with peptide 1 has been studied using dynamic NMR studies, which concludes that a bifurcated hydrogen bonding interaction exists in the molecular interfaces of the assembly. Copyright © 2003 John Wiley & Sons, Ltd.