63473-46-1Relevant academic research and scientific papers
Pd-Catalyzed Site-Selective C(sp2)-H Olefination and Alkynylation of Phenylalanine Residues in Peptides
Zheng, Yong,Song, Weibin
supporting information, (2019/05/08)
Pd-catalyzed site-selective C(sp2)-H olefination and alkynylation of phenylalanine residues in peptides are described. The amino acids within the peptides are used as native bidentate directing groups to facilitate C-H functionalization. This p
Visible-Light-Driven, Copper-Catalyzed Decarboxylative C(sp3)?H Alkylation of Glycine and Peptides
Wang, Chao,Guo, Mengzhun,Qi, Rupeng,Shang, Qinyu,Liu, Qiang,Wang, Shan,Zhao, Long,Wang, Rui,Xu, Zhaoqing
supporting information, p. 15841 - 15846 (2018/11/23)
Despite a well-developed and growing body of work in Cu catalysis, the potential of Cu to serve as a photocatalyst remains underexplored. Reported herein is the first example of visible-light-induced Cu-catalyzed decarboxylative C(sp3)?H alkylation of glycine for preparing α-alkylated unnatural α-amino acids. It merits mentioning that the mild conditions and the good functional-group tolerance allow the modification of peptides using this method. The mechanistic studies revealed that a radical–radical coupling pathway is involved in the reaction.
9-Silafluorenyl Dichlorides as Chemically Ligating Coupling Agents and Their Application in Peptide Synthesis
Aspin, Samuel J.,Taillemaud, Sylvain,Cyr, Patrick,Charette, André B.
supporting information, p. 13833 - 13837 (2016/10/26)
A fundamentally simple, mild, and practical procedure for peptide bond formation is reported that employs a stoichiometric amount of easy-to-access 9-silafluorenyl dichlorides as the coupling agent. Without initial preactivation or elaboration of the carboxylic acid or amine termini of the amino acids, the developed reagent is proposed to act through an unprecedented chemical ligation mechanism, bringing the two coupling partners together before being subsequently eliminated. The desired amides or peptide bonds are thus furnished in good yields and with low to no epimerization.
Native chemical ligation at phenylalanine
Crich, David,Banerjee, Abhisek
, p. 10064 - 10065 (2008/03/12)
Synthesis of erythro-N-Boc-β-mercapto-l-phenylalanine enables native chemical ligation at phenylalanine. In the form of the S-ethyldisulfanyl derivative, the N-Boc amino acid is used to cap a tetrapeptide generated by Fmoc-SPPS. The native chemical ligati
Dipeptidyl nitriles as human dipeptidyl peptidase I inhibitors
Bondebjerg, Jon,Fuglsang, Henrik,Valeur, Kirsten Rosendal,Pedersen, John,Naerum, Lars
, p. 3614 - 3617 (2007/10/03)
Using a dipeptide nitrile scaffold we have identified a potent and selective inhibitor of human dipeptidyl peptidase I.
SYNTHESIS AND SOME BIOLOGICAL PROPERTIES OF ANALOGUE OF ANGIOTENSIN WITH MODIFIED PROLINE STRUCTURE
Prochazka, Zdenko,Ancans, Yuris E.,Myshlyakova, Nataliya V.,Ratkevich, Marita P.,Strazda, Gunta M.
, p. 3008 - 3014 (2007/10/02)
The angiotensin analogue was synthesized by fragment condensation employing the azide method.Proline in the position 7 in this analogue and phenylalanine in the position 8 were substituted with 2--3-phenylpropa
Protected Lactam-Bridged Dipeptides for Use as Conformational Constraints in Peptides
Freidinger, Roger M.,Perlow, Debra Schwenk,Veber, Daniel F.
, p. 104 - 109 (2007/10/02)
General methods have been devised for the synthesis of lactam-constrained dipeptide analogues having five-, six-, and seven-membered rings.Three different paths from protected chiral α-amino acids to lactams involving intramolecular alkylation, intramolecular acylation, and insertion of a one carbon unit by condensation with formaldehyde have been utilized.The first two methods produce chiral products stereospecifically, but considerable racemization occurs in the third route which leads to a 4-oxo-5-amino-1,3-thiazine (13).The products are prepared in good yield and have protecting groups making them suitable for incorporation into higher peptides by methods commonly used.
