17460-97-8

Upstream product

• 2528-15-6 D-valine t-butyl ester 
• 1161-13-3 N-Cbz-L-Phe 
• 2519-21-3 Z-Phe-D-Val-OtBu 
• 117999-33-4 Z-ΔPhe-(S)-Val-OH 

Downstream Products

• 82213-53-4 Z-Phe-D-Val-Pro-OH 
• 82213-52-3 Z-Phe-D-Val-Pro-OBu^t 

Relevant academic research and scientific papers

Epimerization-Free C-Term Activation of Peptide Fragments by Ball Milling

Peptides were produced in high yields and, if any, very low epimerization, by mechanochemical coupling of peptide fragments containing highly epimerization-prone and/or highly hindered amino acids at C-term. Ball milling was clearly identified as the key element enabling one to obtain such results.

Efficient 1,4-Asymetric Induction Utilizing Electrostatic Interaction between Ligand and Substrate in the Asymmetric Hydrogenation of Didehydrodipeptides

Electrostatic interaction between the amino group of the achiral 3-dimethylaminopropylidenebismethylenebis(diphenylphosphine) (1) and the carboxy group of the substrate enable an effective 1,4-asymmetric induction in the RhI-catalysed hydrogenation of didehydrodipeptides, to give (S,S)-or (R,R)-products selectively.The selectivity reached up to 94percent diastereoisomeric excess with acetyl didehydrodipeptides and 92percent with benzyloxycarbonyl substrates.