88719-17-9

Upstream product

• 18942-49-9 Boc-D-Phe-OH 
• 4530-18-1 2-(tert-butoxycarbonylamino)-3-phenylpropionic acid 

Downstream Products

• 88815-84-3 (S)-tert-Butyl 1-Oxo-3-phenyl-1-(pyrrolidin-1-yl)propan-2-ylcarbamate 
• 141468-60-2 7-(N-t-butyloxycarbonyl-D-phenylalanyl)amino-4-chloro-3-(2-bromoethoxy)isocoumarin 
• 141468-82-8 {(R)-1-[3-(3-Bromo-propoxy)-4-chloro-1-oxo-1H-isochromen-7-ylcarbamoyl]-2-phenyl-ethyl}-carbamic acid tert-butyl ester 

Relevant academic research and scientific papers

Electrophilic Activation of Carboxylic Anhydrides for Nucleophilic Acylation Reactions

Nucleophilic acylation of symmetrical carboxylic anhydrides has inherited limitation of reaction efficiency along with relatively poor reactivity. Traditionally, one equivalent carboxylic acid is generated during nucleophilic acylation of a symmetrical anhydride, which always limits the yield of final product to 50percent or less. This is a major drawback, which discourages the use of anhydrides for laboratory or industrial applications. Electrophilic activation of carboxylic anhydride using methanesulfonyl chloride is found to be an efficient method for nucleophilic acylation, which increases product yield by restricting the formation of corresponding acid as a side product. The developed protocol found to be a mild and high yielding methodology for one-pot nucleophilic acylation of carboxylic anhydrides with several type of N- and S-nucleophiles demonstrating appreciable functional group tolerance.

Induced axial chirality in the biphenyl core of the proatropoisomeric, Cα-tetrasubstituted α-amino acid residue Bip in peptides

An induced axial chirality in the biphenyl core of the 2′,1′:1,2;1″,2″:3,4-dibenzcyclohepta-1, 3-diene-6-amino-6-carboxylic acid (Bip) residue, a conformationally labile, atropoisomeric, Cα-tetrasubstituted α-amino acid, was observed by CD and 1H NMR spectroscopic techniques in the linear dipeptides Boc-Bip-Xaa*-OMe where Boc = tert-butoxycarbonyl, OMe = methoxy, and Xaa* = D- and/or L-Ala, -Val, -Leu, -Phe, -(αMe)Val and -(αMe)Leu. Chiral induction was significantly lower in the isomeric dipeptides Boc-Xaa*-Bip-OMe, with the Xaa* residue located at the N-terminus of Bip, as well as in the cyclic dipeptide cyclo-[Bip-L-Ala]. The results obtained in solution were confirmed by X-ray diffraction analysis of a crystalline sample of Boc-(R)-Bip-D-Ala-OMe.