76542-83-1Relevant articles and documents
Fmoc-AA-NH2 Preparation method
-
Paragraph 0045-0046, (2021/10/02)
The invention relates to Fmoc-AA-NH. 2 The invention discloses a preparation method of a polypeptide and belongs to the technical field of polypeptide synthesis. Fmoc-AA-NH of the present invention2 The preparation method comprises: NH. 4 X Is first dissolved in a basic solvent system, and then Fmoc-AA-OSu reaction is added to obtain Fmoc-AA-NH. 2 . Wherein, pH of the reaction is 8 - 9, and AA is an amino acid or an amino acid derivative with only one carboxyl group. NH4 X Is NH. 4 Cl, (NH4)2 SO4 At least one of the foregoing. The base in the basic solvent system is NaHCO. 3 , KHCO3 , Na2 CO3 , K2 CO3 At least one of the foregoing. The solvent system in the alkaline solvent system is THF/H. 2 O, CAN / H2 At least one of O.
Site-Specific Incorporation of Multiple Thioamide Substitutions into a Peptide Backbone via Solid Phase Peptide Synthesis
Yang, Jinhua,Wang, Changliu,Yao, Chaochao,Chen, Chunqiu,Hu, Yafang,He, Guifeng,Zhao, Junfeng
, p. 1484 - 1494 (2020/01/02)
Among various peptide modification strategies, thioamide substitution by replacing the carbonyl oxygen atom of an amide bond with a sulfur atom constitutes an invaluable tool for chemical biology, for use in peptide drug discovery and protein structure-fu
Ynamide-Mediated Thiopeptide Synthesis
Yang, Jinhua,Wang, Changliu,Xu, Silin,Zhao, Junfeng
supporting information, p. 1382 - 1386 (2019/01/08)
Exploration of the full potential of thioamide substitution as a tool in the chemical biology of peptides and proteins has been hampered by insufficient synthetic strategies for the site-specific introduction of a thioamide bond into a peptide backbone. A novel ynamide-mediated two-step strategy for thiopeptide bond formation with readily available monothiocarboxylic acids as thioacyl donors is described. The α-thioacyloxyenamide intermediates formed from the ynamides and monothiocarboxylic acids can be purified, characterized, and stored. The balance between their activity and stability enables them to act as effective thioacylating reagents to afford thiopeptide bonds under mild reaction conditions. Amino acid functional groups such as OH, CONH2, and indole NH groups need not be protected during thiopeptide synthesis. The modular nature of this strategy enables the site-specific incorporation of a thioamide bond into peptide backbones in both solution and the solid phase.
A facile synthesis and crystallographic analysis of N-protected β-amino alcohols and short peptaibols
Jadhav, Sandip V.,Bandyopadhyay, Anupam,Benke, Sushil N.,Mali, Sachitanand M.,Gopi, Hosahudya N.
supporting information; experimental part, p. 4182 - 4187 (2011/06/28)
A facile, efficient and racemization-free method for the synthesis of N-protected β-amino alcohols and peptaibols using N-hydroxysuccinimide active esters is described. Using this method, dipeptide, tripeptide and pentapeptide alcohols were isolated in high yields. The conformations in crystals of β-amino alcohol, dipeptide and tripeptide alcohols were analysed, with a well-defined type III β-turn being observed in the tripeptide alcohol crystals. This method is found to be compatible with Fmoc-, Boc- and other side-chain protecting groups.
Design and synthesis of novel prodrugs of 2′-deoxy-2′-methylidenecytidine activated by membrane dipeptidase overexpressed in tumor tissues
Kohchi, Yasunori,Hattori, Kazuo,Oikawa, Nobuhiro,Mizuguchi, Eisaku,Isshiki, Yoshiaki,Aso, Kohsuke,Yoshinari, Kiyoshi,Shirai, Haruyoshi,Miwa, Masanori,Inagaki, Yukiko,Ura, Masako,Ogawa, Kotaroh,Okabe, Hisafumi,Ishitsuka, Hideo,Shimma, Nobuo
, p. 2241 - 2245 (2008/02/03)
DNA microarray analysis comparing human tumor tissues with normal tissues including hematopoietic progenitor cells resulted in identification of membrane dipeptidase as a prodrug activation enzyme. Novel prodrugs of 2′-deoxy-2′-methylidenecytidine (DMDC)
