Cyclo[Dip-Tza-Leu-D-N(Me)Val-D-Leu] forms a conformationally locked macrocycle containing noncanonical residues and N-methylation. Such features restrict backbone motion and enhance resistance to proteolysis. Researchers probe its interaction with hydrophobic pockets and structured protein surfaces. Applications include cyclic-peptidomimetic design, ligand-scaffold optimization, and stability-focused structure-activity studies.
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