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Circular dichroism and nuclear magnetic resonance spectroscopy are utilized to perform the conformational analysis of hemopressin and its truncated, biologically active fragments and molecular docking calculations are used to study the binding modes of hemopressin peptide to the cannabinoid [CB.sub.1] receptor. The conformational data indicated that regular turn structures in the central portion of hemopressin and its fragments are critical for an effective interaction with the receptor molecular docking calculations provides new insight into new chemical scaffolds for the design of new [CB.sub.1].

The article discusses a new approach, where in the i to i+4 intramolecular side-chain to side-chain azide-alkyne 1,3-dipolar cycloaddition of side chains is employed for the synthesis of a cyclic peptide. The cyclopeptides thus obtained are shown to exhibit similar bioactivities.

The molecular mechanism of the interaction between 2,3'-cyclic nucleotide-3'-phosphodiesterase (CNP) and the plasma membrane is examined by using a general model to interpret the structural bases of prenylated proteins binding to the membrane. The studies have shown that the presence of the lipidic tail is necessary for the peptide to be folded and properly positioned on the membrane surface.