132682-05-4

Upstream product

• 5497-76-7 L-proline tert-butyl ester hydrochloride 
• 367274-56-4 Z-Aib-F 
• 15030-72-5 Z-Aib-OH 
• 83283-35-6 Proline tert-butyl ester dibenzenesulfimide salt 
• 2812-46-6 proline tert-butyl ester 

Downstream Products

• 132682-09-8 H-Aib-Pro-OtBu*HCl 
• 128422-13-9 Z-L-Leu-Aib-Pro-OtBu 

Relevant academic research and scientific papers

Metal-free approach for hindered amide-bond formation with hypervalent iodine(iii) reagents: application to hindered peptide synthesis

A new bio-inspired approach is reported for amide and peptide synthesis using α-amino esters that possess a potential activating group (PAG) at the ester residue. To activate the ester functionality under mild metal-free conditions, we exploited the facile dearomatization of phenols with hypervalent iodine(iii) reagents. Using a pyridine-hydrogen fluoride complex, highly reactive acyl fluoride intermediates can be successfully generated, thereby allowing for the smooth formation of sterically hindered amides and peptides from bulky amines and α-amino esters, respectively.

Peptide Mechanosynthesis by Direct Coupling of N-Protected α-Amino Acids with Amino Esters

In view of developing alternatives to classical peptide synthesis strategies that suffer from low efficacy and negative environmental impact, the reactivity of N-protected α-amino acids, amino esters, and N-ethyl-N′-(3-dimethylaminopropyl)carbodiimide was

PyBOP and PyBroP: Two reagents for the difficult coupling of the α,α-dialkyl amino acid, Aib

The difficult coupling of α-aminoisobutyric acid (Aib) was carried out using PyBOP and PyBroP in a comparative study with BOP and BroP. These reagents gave good results under simple conditions (one pot, r.t., 1h). Coded amino acids could be coupled with Aib using PyBOP under standard conditions of peptide synthesis without racemization whereas the coupling of two Aib residues required PyBroP/DMAP. A fragment containing an Aib C-terminal could be coupled without epimerization of the penultimate residue.