6960-35-6Relevant academic research and scientific papers
C(sp3) -C(sp2) Method for constructing key and β - aryl amino acid preparation method
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Paragraph 0051; 0057-0059; 0061, (2021/10/27)
The invention provides C. (sp3) - C(sp2) A method for constructing a key and β -aryl amino acid relates to the technical field of chemical substance synthesis and transition metal application, which comprises β-C amino acid. (sp3) Ring carbon C in place of phenolic hydroxyl group(sp2) A method of constructing C-C keys by direct coupling. The process will contain inactive β-C. (sp3) Amino acids of - H and ligands L of specific structure1 The tetradentate chelate is generated by complexation with bivalent nickel, and the amino acid labile β-C is completed under the catalysis of palladium with phenolic ester under basic conditions. (sp3) - H Aryl, proton transfer and the like are reacted to achieve C. (sp3) - C(sp2) Construction of a bond, finally hydrolytically releasing β-C aryl amino acid and ligand L1 C. (sp3) - C(sp2) The key construction method is simple and convenient to operate. The method has the advantages of low cost, strong reaction universality, high yield and stereoselectivity. The synthetic method provides a novel method for preparing various non-natural β - aryl amino acids, and provides a novel method for amino acidification/peptide modification of phenolic compounds with biological activity, and provides a novel approach and selection for the design and synthesis of new drugs.
Suzuki-Miyaura Diversification of Amino Acids and Dipeptides in Aqueous Media
Willemse, Tom,Van Imp, Karolien,Goss, Rebecca J. M.,Van Vlijmen, Herman W. T.,Schepens, Wim,Maes, Bert U. W.,Ballet, Steven
, p. 2055 - 2070 (2015/11/24)
The Suzuki-Miyaura derivatisation of free amino acids, peptides and proteins is an attractive area with considerable potential utility for medicinal chemistry and chemical biology. Here we report the modification of unprotected and Boc-protected aromatic amino acids and dipeptides in aqueous media, enabling heteroarylation and vinylation. We systematically investigate the impact of the peptide backbone and adjacent amino acid residues upon the reaction. Our studies reveal that although asparagine and histidine hinder the reaction, by utilising dppf, a ferrocene-based bidentate phosphine ligand, cross coupling of halophenylalanine or halotryptophan adjacent to such a residue could be enabled. Our studies reveal dppf to have good compatibility with all unprotected, proteinogenic amino acid side chains.
