73538-53-1Relevant academic research and scientific papers
Phosphorus pentoxide for amide and peptide bond formation with minimal by-products
Erapalapati, Venkataramana,Hale, Umatai A.,Madhavan, Nandita
supporting information, (2019/11/21)
Phosphorus pentoxide and DMAP are used for amide bond formation from carboxylic acids and amines. Dipeptides and amides have been synthesized using this reagent in 42–77% yields and >99% ees. The protocol is attractive as it occurs at ambient temperature, the formation of organic by-products is minimal and the reagent can be readily quenched using water. Furthermore, excellent enantioselectivities are observed without the use of harsh triazole based additives.
HMDO-promoted peptide and protein synthesis in ionic liquids
Duan, Jianli,Sun, Yao,Chen, Hao,Qiu, Guofu,Zhou, Haibing,Tang, Ting,Deng, Zixin,Hong, Xuechuan
, p. 7013 - 7022 (2013/08/23)
Hexamethyldisiloxane (HMDO) has been developed to efficiently promote the metal-free direct coupling of an amino function of one cysteine-free peptide or protein and a C-terminal thioester of the second peptide in ionic liquids. The amide-coupling reaction proceeds smoothly under mild conditions to afford the corresponding products in good to excellent yields (63-94%). Peptide couplings were also achieved using in-situ-generated thioesters by the thioesterification of oxo esters.
Enantioselective Synthesis of erythro-β-Hydroxy-L-histidine, the Pivotal Amino Acid of Bleomycin-Fe(II)-O2 Complex
Owa, Takashi,Otsuka, Masami,Ohno, Masaji
, p. 83 - 86 (2007/10/02)
erythro-β-Hydroxy-L-histidine, a novel amino acid constituent of bleomycin, has been synthesized enantioselectively via the reaction of (N-pyruvylideneglycyl-D-phenylalaninato)copper(II) with imidazole-4-carbaldehyde.
Papain Catalysed Peptide Synthesis: Control of Amidase Activity and the Introduction of Unusual Amino Acids
Barbas, Carlos F. III,Wong, Chi-Huey
, p. 533 - 534 (2007/10/02)
Procedures for the papain catalysed synthesis of peptides containing D-amino acids and derivatives with control of the enzyme's amidase activity have been developed.
