- Synthesis method of amide nitrogen trifluoromethyl compound
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The invention discloses a synthesis method of an amide nitrogen trifluoromethyl compound. The synthesis method comprises the following step: carrying out trifluoromethylation reaction on a compound shown in a formula a1 or a formula a2 and a trifluoromethylation reagent in an organic solvent under the action of a fluorination reagent, an oxidant, silver oxysalt and a pyridine ligand, so as to obtain a target compound shown in a formula b1 or a formula b2. According to the invention, trifluoromethylation reaction can be directly carried out on an amide compound shown as a formula a1 or a sulfonamide compound shown as a formula a2 so as to obtain the amide nitrogen trifluoromethyl compound shown in the formula b1 or the sulfamide nitrogen trifluoromethyl compound shown in the formula b2. Themethod has the advantages of simple operation, easily available raw materials, low cost, safety, environmental protection, mild reaction conditions, easy realization of large-scale production, and the like, and is of great significance to the industrial application of the amide nitrogen trifluoromethyl compound.
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Paragraph 0040; 0065-0069
(2020/07/15)
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- Synthesis of L-Alanyl-3-O-(β-D-xylopyranosyl)-L-seryl-glycyl-L-isoleucine. Direct Glycosydation of Peptides
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Glycosidation of the tetrapeptide 8 either with 1,2,3,4-tetra-O-acetyl-β-D-xylopyranose (1) under catalysis of trimethylsilyl triflate or with ethyl 2,3,4-tri-O-benzoyl-1-thio-β-D-xylopyranoside (4) using DMTST as promotor, leads to the O-glycopeptides 10 and 9.Deblocking of 10 affords the glycopeptide L-Ala-3-O-(β-D-Xylp)-L-Ser-Gly-L-Ile (11), which represents the N-terminal amino acid sequence 3 to 6 of the protein core of a proteodermantan sulfate.
- Paulsen, Hans,Brenken, Mathias
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p. 649 - 654
(2007/10/02)
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- STUDIES OF BITTER PEPTIDES FROM CASEIN HYDROLYZATE - VI. SYNTHESES AND BITTER TASTE OF BPIc (VAL-TYR-PRO-PHE-PRO-PRO-GLY-ILE-ASN-HIS) AND ITS ANALOGS AND FRAGMENTS.
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In order to investigate the relationship between chemical structure and bitter taste, the bitter peptide BPIc (Val-Tyr-Pro-Phe-Pro-Pro-Gly-Ile-Asn-His) isolated from casein hydrolyzate by Minamiura et al. and its analogs and fragments were synthesized. BPIc, whose threshold value of bitter taste was 0. 05 mm, was found to be one of the most bitter compounds, like quinine and phenylthiourea. However, left bracket Gly**5**,**6 right bracket - and left bracket Gly**9**,**1**0 right bracket -BPIc, and N-terminal octa- and heptapeptide fragments of BPIc possessed much weaker bitterness than BPIc. The results suggested that 5,6-proline and the basic nature of C-terminal are necessary for the strong bitterness exhibited by BPIc.
- Kanehisa
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