70396-23-5

Upstream product

• 15761-38-3 L-N-Boc-Ala 
• 87892-68-0 methyl L-alanyl-L-phenylalanine trifluoroacetate 
• 7524-50-7 methyl (2S)-2-amino-3-phenylpropanoate hydrochloride 
• 2280-66-2 N-tert-butyloxycarbonylalanylphenylalanine methyl ester 

Downstream Products

• 56133-10-9 N-(tert-butoxycarbonyl)-L-alanyl-L-alanyl-L-phenylalanine 
• 1590380-86-1 C₃₂H₄₄N₄O₁₀ 
• 1590380-90-7 C₂₃H₂₆N₄O₇ 
• 1590380-71-4 C₃₂H₃₇N₅O₇ 
• 1590380-72-5 C₂₅H₃₁N₅O₇ 
• 1590380-73-6 C₂₆H₃₁N₅O₈ 
• 1590380-94-1 C₂₉H₃₈N₆O₈ 
• 1590380-75-8 C₂₄H₃₀N₆O₆*C₂HF₃O₂ 
• 825615-54-1 (S)-2-[(3S,4R)-3-((S)-1-{(S)-2-[(S)-2-((S)-2-tert-Butoxycarbonylamino-propionylamino)-propionylamino]-3-phenyl-propionylamino}-ethyl)-2-oxo-4-phenyl-azetidin-1-yl]-4-methyl-pentanoic acid methyl ester 
• 825615-51-8 (S)-2-[(3R,4S)-3-((S)-1-{(S)-2-[(S)-2-((S)-2-tert-Butoxycarbonylamino-propionylamino)-propionylamino]-3-phenyl-propionylamino}-ethyl)-2-oxo-4-phenyl-azetidin-1-yl]-4-methyl-pentanoic acid methyl ester 

Relevant academic research and scientific papers

Furan-based locked Z -vinylogous γ-amino acid stabilizing protein α-turn in water-soluble cyclic α3γ tetrapeptides

Described here is the design, synthesis, and conformational analysis of cyclic tetrapeptides (CTPs) with α3γ architecture containing a furan-based locked Z-vinylogous amino acid (Vaa). This unnatural amino acid locks into a γ-turn that induces

Palladium catalyzed reductive deprotection of alloc: Transprotection and peptide bond formation

N-allyloxycarbonyl group could be efficiently removed using sodium borohydride as hydride donor in the presence of catalytic amount of palladium (0). The conditions were applied to chemoselective protecting group transformation (transprotection) and peptide bond formation.

SEGMENT COUPLING IN PEPTIDE SYTHESIS-II A SIMPLE PREDICTIVE EQUATION CORRELATING RACEMIZATION AND PRIMARY STRUCTURE

A predictive equation based on extrathermodynamic assumptions is proposed, that allows the prediction of the degree of epimerization in tripeptide model reactions of condensation of peptide segments as a function of the primary structure.The experimental