119206-32-5

Upstream product

• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 24608-52-4 tert-butyl chloroformate 
• 63-91-2 L-phenylalanine 
• 24424-99-5 di-tert-butyl dicarbonate 

Downstream Products

• 66714-00-9 ethyl (tert-butoxycarbonyl)-L-phenylalanyl-L-phenylalaninate 
• 66605-57-0 (S)-N-tert-butoxycarbonyl-2-amino-3-phenylpropanol 
• 140171-07-9 Boc-Phe-Phe-MePhe-Gly-Ψ(CH2-NH)-Leu-Met-NH2 
• 140170-93-0 Boc-Phe-Phe-Sar-Ψ(CH2-NH)-Leu-Met(O2)-NH2 
• 140171-06-8 Boc-Phe-MePhe-Gly-Ψ(CH2-NH)-Leu-Met-NH2 
• 140170-99-6 Boc-Phe-Val-Gly-Ψ(CH2-NH)-Leu-Nle-NH2 
• 140170-92-9 Boc-Phe-Sar-Ψ(CH2-NH)-Leu-Met(O2)-NH2 
• 70462-58-7 benzyl (tert-butoxycarbonyl)-L-phenylalanyl-L-prolinate 

Relevant academic research and scientific papers

Use of di-tert-butyl-dicarbonate both as a protecting and activating group in the synthesis of dipeptides

Amide formation from amino acids was achieved in an easy and convenient one-pot procedure using di-tert-butyl dicarbonate both as a protecting and an activating agent. A number of dipeptides have been synthesized in good yields. Copyright Taylor & Francis Group, LLC.

Simple and efficient synthesis of Fmoc/Boc/Cbz-protected-β-amino alcohols and peptidyl alcohols employing Boc2O

An efficient method for the activation of Fmoc/Boc/Cbz-protected amino acids using Boc2O and the reduction of the in situ generated carbonic-carbonic anhydride to their corresponding 1β-amino alcohols using sodium borohydride has been described. The method is simple, rapid and free from racemization. Besides, the protocol is also extended for the conversion of N-urethane protected peptide acids to their corresponding alcohols. Copyright

Synthesis and biological activities of neurokinin pseudopeptide analogues containing a reduced peptide bond

A series of pseudopeptides, analogues of neurokinin selective agonists, in which a peptide bond was replaced by a (CH2NH) bond were synthesized. The biological activities of these compounds were determined on selective pharmacological preparations: the dog carotid artery for NK-1, the rabbit pulmonary artery devoid of endothelium for the NK-2 and the rat portal vein for the NK-3 receptors. The results reported in this study indicate that insertion of a pseudopeptide bond in various positions of these selective agonists resulted in a great decrease in potency compared to the parent compounds. Furthermore, the selectivity of agonists is maintained by the use of a methylene amino group in position 9-10 (Sar) for the NK-1 or in position 7-8 (MePhe) for the NK-3 selective compound. The selectivity is greatly diminished for the NK-2 analogues.

SYNTHESIS OF A HEPTAPEPTIDE WITH SEQUENCE 17 - 23 OF HUMAN CALCITONIN

Two schemes for the synthesis of a peptide with sequence 17 - 23 of human calcitonin with the minimum protection of the lateral functions of the amino acids are proposed.