- Synthesis method of multi-configuration long-chain phenyl amino acid compound
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The invention relates to a method for synthesizing a multi-configuration long-chain phenyl amino acid compound. The method comprises the following steps: reacting a compound shown in a formula I witha compound shown in a formula II or an isomer thereof in
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Paragraph 0071-0077; 0085-0091
(2021/03/05)
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- Effective synthesis of optically active 3-phenyl-3-(3-trifluoromethyl) diazirinyl bishomophenylalanine derivatives
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Effective incorporation of phenyldiazirine moiety on the acyl residue of L- and D- glutamic acid by Friedel-Crafts reactions with triflic acid developed simple preparation of bishomophenylalanine (bhPhe) for aromatics, which added a
- Murai, Yuta,Hatanaka, Yasumaru,Kanaoka, Yuichi,Hashimoto, Makoto
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body text
p. 359 - 364
(2009/12/03)
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- Controlling diastereoselectivity in the reactions of enantiomerically pure α-bromoacyl-imidazolidinones with nitrogen nucleophiles: Substitution reactions with retention or inversion of configuration
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Diastereoselective substitution reactions of α-bromoacyl- imidazolidinones with nitrogen nucleophiles can be promoted with either retention or inversion of configuration by carrying out reactions under epimerising or non-epimerising conditions. The Royal Society of Chemistry 2005.
- Treweeke,Hitchcock,Pardoe,Caddick
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p. 1868 - 1870
(2007/10/03)
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- Inhibitors of cathepsin S
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The present invention provides compounds, compositions and methods for the selective inhibition of cathepsin S. In a preferred aspect, cathepsin S is selectively inhibited in the presence of at least one other cathepsin isozyme (e.g., cathespin K). The pr
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- Kinetic Resolution of Unnatural and Rarely Occuring Amino Acids: Enantioselective Hydrolysis of N-Acyl Amino Acids Catalyzed by Acylase I
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Acylase I (aminoacylase; N-acylamino-acid amidohydrolase, EC 3.5.1.14, from porcine kidney and the fungus Aspergillus) is broadly applicable enzymatic catalyst for the kinetic resolution of unnatural and rarely occuring α-amino acids.Its enantioselectivity for the hydrolysis of N-acyl L-α-amino acids is nearly absolute, yet it accepts substrates having a wide range of structure and functionality.This paper reports the initial rates of enzyme-catalyzed hydrolysis of over 50 N-acyl amino acids and analogues, the stabilities of the enzymes in aqueous and aqueous/organic solutions, and the effects of different acyl groups and metal ions on the rates of enzymatic hydrolysis.Eleven α-amino and α-methyl α-amino acids were resolved on a 2-29-g scale.Crude L- and D-amino acid products had generally >90percent ee.The utility of resolved amino acids as chiral synthons was illustrated by the preparation of (R)- and (S)-1-butene oxide and the diastereoselective (cis:trans, 7-8:1) iodolactonization of three 2-amino-4-alkenoic acid derivatives.
- Chenault, H. Keith,Dahmer, Juergen,Whitesides, George M.
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p. 6354 - 6364
(2007/10/02)
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