title: On resin side-chain cyclization of complex peptides using CuAAC.
abstract: Triazole tethers have been explored for stabilization of secondary structures in peptides. Despite the utility of this approach, cyclization efficiency in complex peptides remains a significant challenge. A robust, on-resin protocol for side chain to side chain macrocyclization by CuAAC is described. This protocol was applied to the synthesis of a series of 21 amino acid helical peptides presenting a binding dipeptide motif from the membrane proximal external region (MPER) of HIV-1 gp41.
authors.affiliation: Department of Chemistry, The Scripps Research Institute, La Jolla, California 92037, United States.
authors.forename: Sampat
authors.initials: S
authors.lastname: Ingale
authors.forename: Philip E
authors.initials: PE
authors.lastname: Dawson
mesh_terms: D000595:Amino Acid Sequence; D002942:Circular Dichroism; D003300:Copper / Q000737:chemistry; D003500:Cyclization; D015700:HIV Envelope Protein gp41 / Q000737:chemistry* / Q000378:metabolism; D015497:HIV-1 / Q000737:chemistry; D015394:Molecular Structure; D010446:Peptide Fragments / Q000737:chemistry* / Q000378:metabolism; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism; D014230:Triazoles / Q000138:chemical synthesis* / Q000737:chemistry
chemical_list: D015700:HIV Envelope Protein gp41; C534067:HIV-1 envelope protein gp41 (649-683); D010446:Peptide Fragments; D010455:Peptides; D014230:Triazoles; D003300:Copper