83291-07-0Relevant academic research and scientific papers
Acceptor-Controlled Transfer Dehydration of Amides to Nitriles
Okabe, Hiroyuki,Naraoka, Asuka,Isogawa, Takahiro,Oishi, Shunsuke,Naka, Hiroshi
supporting information, p. 4767 - 4770 (2019/06/17)
Palladium-catalyzed dehydration of primary amides to nitriles efficiently proceeds under mild, aqueous conditions via the use of dichloroacetonitrile as a water acceptor. A key to the design of this transfer dehydration catalysis is the identification of an efficient water acceptor, dichloroacetonitrile, that preferentially reacts with amides over other polar functional groups with the aid of the Pd catalyst and makes the desired scheme exergonic, thereby driving the dehydration.
Peptide ligation by chemoselective aminonitrile coupling in water
Canavelli, Pierre,Islam, Saidul,Powner, Matthew W.
, p. 546 - 549 (2019/07/18)
Amide bond formation is one of the most important reactions in both chemistry and biology1–4, but there is currently no chemical method of achieving α-peptide ligation in water that tolerates all of the 20 proteinogenic amino acids at the peptide ligation site. The universal genetic code establishes that the biological role of peptides predates life’s last universal common ancestor and that peptides played an essential part in the origins of life5–9. The essential role of sulfur in the citric acid cycle, non-ribosomal peptide synthesis and polyketide biosynthesis point towards thioester-dependent peptide ligations preceding RNA-dependent protein synthesis during the evolution of life5,9–13. However, a robust mechanism for aminoacyl thioester formation has not been demonstrated13. Here we report a chemoselective, high-yielding α-aminonitrile ligation that exploits only prebiotically plausible molecules—hydrogen sulfide, thioacetate12,14 and ferricyanide12,14–17 or cyanoacetylene8,14—to yield α-peptides in water. The ligation is extremely selective for α-aminonitrile coupling and tolerates all of the 20 proteinogenic amino acid residues. Two essential features enable peptide ligation in water: the reactivity and pKaH of α-aminonitriles makes them compatible with ligation at neutral pH and N-acylation stabilizes the peptide product and activates the peptide precursor to (biomimetic) N-to-C peptide ligation. Our model unites prebiotic aminonitrile synthesis and biological α-peptides, suggesting that short N-acyl peptide nitriles were plausible substrates during early evolution.
Rhodium-catalyzed enantioselective hydrogenation of α-amino acrylonitriles: an efficient approach to synthesizing chiral α-amino nitriles
Li, Xiuxiu,You, Cai,Yang, Yusheng,Wang, Fangyuan,Li, Shuailong,Lv, Hui,Zhang, Xumu
supporting information, p. 1313 - 1316 (2017/02/05)
An efficient rhodium-catalyzed asymmetric hydrogenation of α-amino acrylonitriles has been developed, affording α-acylamino nitriles with high yields and excellent enantioselectivities (up to 99% yield and >99% ee). This novel methodology provides an effi
Synthesis of isotopically labeled P-site substrates for the ribosomal peptidyl transferase reaction
Zhong, Minghong,Strobel, Scott A.
, p. 603 - 611 (2008/09/17)
(Chemical Equation Presented) Isotopomers of the ribosomal P-site substrate, the trinucleotide peptide conjugate CCA-pcb (Zhong, M.; Strobel, S. A. Org. Lett. 2006, 8, 55-58), have been designed and synthesized in 26-35 steps. These include individual iso
Desilylative elimination of the quinazolinone ring from 1-(4-oxoquinazolin-3-yl)-2-silylaziridines; preparation of an N-H aziridine in high enantiomeric excess by in situ nucleophilic addition to the derived azirine
Atkinson, Robert S.,Coogan, Michael P.,Lochrie, Ian S. T.
, p. 897 - 900 (2007/10/03)
Aziridination of vinylsilanes PhCH=CHSiR3 (R = Me, Et, Ph) with enantiopure 3-acetoxyaminoquinazolinone 11 gives the corresponding aziridines 12 [diastereoisomer ratio (dr) 10:1], 18 (dr 13:1) and 20 (dr 2:1). Desilylative elimination of the quinazolinone from these aziridines by caesium fluoride in the presence of cyanide gives aziridine 14 by cyanide addition to the 3-unsubstituted azirine 13, produced in situ. Acylation of aziridine 14 with (S)-acetoxypropionyl chloride gives N-acylaziridine 16; the good correlation between the diastereoisomer ratios of aziridines 12, 18 and 20 and those of the N-acylaziridine 16 produced in each case suggests that intermediate azirine 13 is configurationally stable.
Preparation of N-H aziridines in high enantiomeric excess by in situ aziridine-azirine-aziridine interconversion
Atkinson, Robert S.,Coogan, Michael P.,Lochrie, Ian S. T.
, p. 789 - 790 (2007/10/03)
Aziridine 6 is produced highly diastereoselectively by treatment of enantiopure 3-acetoxyaminoquinazolinone 4 (Q*NHOAc) with β-trimethylsilylstyrene: desilylative elimination of Q* and in situ addition of cyanide to the intermediate azirine gives the NH-a
Carboxyl-Modified Amino Acids and Peptides as Protease Inhibitors
Thompson, Stewart A.,Andrews, Peter R.,Hanzlik, Robert P.
, p. 104 - 111 (2007/10/02)
Several types of carbonyl-modified amino acids and peptides were prepared in forms having N-terminal modifications (carrier fragments) suitable for one of several representative protease enzymes, and their inhibitory action toward those enzymes were evalu
