1217266-35-7

Basic information

• Product Name: Nα-Ac-Lys-Gly-Nva(δ-N3)-Ser-Ile-Gln-Nle(δ-yl)-Leu-Arg-NH2
• Synonyms: Nα-Ac-Lys-Gly-Nva(δ-N3)-Ser-Ile-Gln-Nle(δ-yl)-Leu-Arg-NH2
• CAS NO: 1217266-35-7
• Molecular Weight: 1119.34
• Mol File: 1217266-35-7.mol
• Article Data: 1

Chemical Properties

• CAS DataBase Reference: Nα-Ac-Lys-Gly-Nva(δ-N3)-Ser-Ile-Gln-Nle(δ-yl)-Leu-Arg-NH2(CAS DataBase Reference)
• NIST Chemistry Reference: Nα-Ac-Lys-Gly-Nva(δ-N3)-Ser-Ile-Gln-Nle(δ-yl)-Leu-Arg-NH2(1217266-35-7)
• EPA Substance Registry System: Nα-Ac-Lys-Gly-Nva(δ-N3)-Ser-Ile-Gln-Nle(δ-yl)-Leu-Arg-NH2(1217266-35-7)

Safety Data

• Hazardous Substances Data: 1217266-35-7(Hazardous Substances Data)

Upstream product

• 1097192-04-5 N^α-(9-fluorenylmethyloxycarbonyl)-azido-L-ornithine 
• 1097192-06-7 2S-{[(9H-fluorenyl-9-ylmethoxy)carbonyl]amino}-7-octynoic acid 
• 29022-11-5 N-(fluoren-9-ylmethoxycarbonyl)glycine 
• 35661-60-0 Fmoc-Leu-OH 
• 108-24-7 acetic anhydride 
• 71989-23-6 Fmoc-Ile-OH 
• 73724-45-5 N-(9H-fluoren-9-ylmethoxycarbonyl)-L-serine 
• 71989-20-3 N₂-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-glutamine 
• 75932-02-4 N-2,N-6-bis(9-fluorenylmethyloxycarbonyl)-L-lysine 

Relevant articles and documents

Cui catalyzed azide-alkyne intramolecular i-to-(i+4) side-chain-to-SideChain cyclization promotes the formation of Helix-Like secondary structures

A solid-phase assembly of model peptides derived from human parathyroid, hormone-related protein (11-19) containing ω-azido- and ω-yl-α-amino acid residues in positions i and i+4 was cyclised in solution by an intramolecular CuI-catalyzed azide-alkyne 1,3-dipolar Huisgen cycloaddition. These series of heterodetic cyclo-nonapeptides varied in the size of the disubstituted 1,2,3-triazolyl-containing bridge, the location and the orientation of the 1,2,3-triazolyl moiety within the bridge. The 1,2,3-triazolyl moiety, presented at either 1,4or 4,1-orientation, is flanked, by side chains containing 1-4 CH2 groups that result in bridges comprised, from 4-7 CH2 groups connecting residues 13 and 17. Comprehensive conformational analysis employing CD, NMR and molecular dynamics reveals the conformational propensities of these heterodetic cyclo-nonapeptides. Cyclo-nonapeptides containing either the 7 methylene bridge (VII and. VIII) or the 4 methylene bridge (II) are unstructured in structure-promoting solvent. Cyclo-nonapeptide I in which the 1,4-disubstituted 1,2,3-triazolyl is flanked by 3 and 1 CH2 groups in proximity to the respective residues 13 and 17, is stabilized in a noncanonical structure. All the other heterodetic cyclo-nonapeptides (III-VI) in which the 1,2,3-triazolyl is flanked by a total of 5 or 6 CH2 groups nicely accommodate a-helical structures and reproduce very closely the helical structure stabilized by the analogous cyclo-nonapeptide in which Lys13 and Asp17 are bridged by the isosteric lactam. These studies suggest that the bioorthogonal i-to-(i+4) side-chain-to-side-chain cyclization via the prototypic click reaction offers a new and powerful approach for generating stable helix mimetic struc-tures