3496-41-1Relevant articles and documents
Ethyl 2-(tert-butoxycarbonyloxyimino)-2-cyanoacetate (Boc-Oxyma) as coupling reagent for racemization-free esterification, thioesterification, amidation and peptide synthesis
Thalluri, Kishore,Nadimpally, Krishna Chaitanya,Chakravarty, Maharishi Parasar,Paul, Ashim,Mandal, Bhubaneswar
supporting information, p. 448 - 462 (2013/05/09)
Here we report the synthesis and utility of ethyl 2-(tert- butoxycarbonyloxyimino)-2-cyanoacetate (Boc-Oxyma) as an efficient coupling reagent for racemization-free esterification, thioesterification, amidation reactions and peptide synthesis that uses equimolar amounts of acids and alcohols, thiols, amines or amino acids, respectively. Its application to solid phase as well as solution phase peptide synthesis is also demonstrated and a mechanistic investigation is discussed. Boc-Oxyma is similar to the well known coupling agent COMU {1-[1-cyano-2-ethoxy-2-oxoethylideneaminooxy)- dimethylaminomorpholino] uronium hexafluorophosphate} in terms of its high reactivity and mechanism of action. However, it is not only much easier to prepare, but also to recover and reuse, thereby generating far less chemical waste.
Catalyst and solvent-free amidation of inactive esters of N-protected amino acids
Nadimpally, Krishna Chaitanya,Thalluri, Kishore,Palakurthy, Nani Babu,Saha, Abhijit,Mandal, Bhubaneswar
supporting information; experimental part, p. 2579 - 2582 (2011/06/21)
A catalyst free procedure for the preparation of amides from inactive esters of N-protected amino acids and various amines is demonstrated under mild reaction conditions. Our effort to recover excess amine and generated alcohol is an approach towards environment friendly and cost effective synthesis under easy operational conditions.
A Mechanism for bitter Taste Sensibility in Peptides
Ishibashi, Norio,Kouge, Katsushige,Shinoda,Ichizo,Kanehisa, Hidenori,Okai, Hideo
, p. 819 - 828 (2007/10/02)
To estimate the steric distance between the bitter taste determinant sites in peptides, some cyclic dipeptides, amino acid anilides, amino acid cyclohexylamides, and benzoyl amino acids were synthesized and their tastes were evaluated.The diketopiperazine ring of cyclic dipeptides acted as a bitter taste determinant site due to its hydrophobicity.The steric distance between 2 sites was estimated as 4.1 Angstroem from the molecule models of cyclic dipeptides composed of typical amino acids in the bitter peptides.Due to the hypothesis of two bitter taste determinant sites, which bind with the bitter taste receptor via a "binding unit" and a "stimulating unit," a mechanism for the bitterness in peptides was postulated.