194471-84-6Relevant articles and documents
Introduction of cyclically constrained γ-residues stabilizes an α-peptide hairpin in aqueous solution
Lengyel, George A.,Eddinger, Geoffrey A.,Horne, W. Seth
supporting information, p. 944 - 947 (2013/04/10)
The synthesis and structural characterization of hybrid α/γ-peptides resulting from a 1:1 α→γ residue substitution at cross-strand positions in a hairpin-forming α-peptide sequence are described. Cyclically constrained γ-residues based on 1,3-substituted
Opioid deltorphin C analogues containing cis- or trans-2- or 3- or 4- aminocyclohexanecarboxylic acid residues
Marastoni, Mauro,Guerrini, Remo,Balboni, Gianfranco,Salvadori, Severo,Fantin, Giancarlo,Fogagnolo, Marco,Lazarus, Lawrence H.,Tomatis, Roberto
, p. 6 - 12 (2007/10/03)
The solid phase synthesis, based on the Fmoc chemical protocol, was used to prepare ten deltorphin C (Del-C; H-Tyr-D-Ala-Phe-Asp-Val-Val-Gly-NH2) analogues containing cis- and trans- 2 or 3- or 4- aminocyclohexanecarboxylic acid (ACCA) residues at position 2, ACCA-peptides showed high resistance to degradation by plasma or brain enzymes, negligible affinity for the κ- binding site and modest δ- and/or μ-receptor affinities. Both [cis-3- ACCA2]Del-C analogues and one trans isomer are the only deltorphin analogues of this series exhibiting an appreciable δ-affinity and selectivity. These data suggest that the presence of a conformationally constrained ACCA residue in position 2 of the 'message' sequence of deltorphin C is slightly tolerated.
