276248-50-1Relevant academic research and scientific papers
PROCESS FOR PRODUCING SOLID AMINO ACID
-
Paragraph 0056, (2014/12/09)
The problem to be solved by the present invention is to ea lily and efficiently produce an amino acid having 2 to 7 carbon atoms as a high-purity solid without complicated operation, which is useful as a synthetic intermediate for medicines or agrochemicals. The present invention is characterized in comprising a step of precipitating solid amino acid with high purity. In the present invention, the by-produced salt composed of the sulfonic acid and the amine was removed to the mother liquor by reacting an amine with a sulfonic acid salt of amino acid in an aprotic polar solvent, or by reacting a sulfonic acid with an amine salt of amino acid in an aprotic polar solvent. The sulfonic acid salt of amino acid, for example, may be produced by reacting a N-(tert-butoxycarbonyl) amino acid with a sulfonic acid, or by reacting an amino acid tert-butyl ester with a sulfonic acid.
HETEROARYLAMIDE LOWER CARBOXYLIC ACID DERIVATIVE
-
Page/Page column 301, (2009/02/10)
To provide a novel compound which has S1P receptor agonistic activity, exhibits excellent immunosuppressing effect, gives less adverse side effects, and can be orally administered. The invention provides a compound represented by general formula (I) (wherein A is a single bond, -O-, or - CH2-; R1 represents a hydrogen atom or a C1-C6 alkyl group, and V represents any one group selected from among the following groups (1) to (3) : (1) -G1-, (2) -G2-N(R2) -G3-, and (3) a group represented by formula 2, wherein each of Z1 and Z2 represents a hydrogen atom or a C1-C6 alkyl group, Z3 represents a hydrogen or the like, Q represents -CH2-O- or the like, and Y represents a group represented by foumula 3, a salt thereof, or a solvate thereof.
Stereochemical control of hairpin formation in β-peptides containing dinipecotic acid reverse turn segments
Chung, Yong Jun,Huck, Bayard R.,Christianson, Laurie A.,Stanger, Heather E.,Krauthaeuser, Susanne,Powell, Douglas R.,Gellman, Samuel H.
, p. 3995 - 4004 (2007/10/03)
We examine the relationship between covalent structure and conformational propensity among a series of β-amino acid tetramers. These experiments focus on the hairpin folding motif. Among conventional peptides, the minimum increment of β-sheet secondary structure is a 'β-hairpin,' in which two strands are connected via a short loop. The present studies are aimed at optimizing hairpin stability among β-peptides. Previous work from our laboratory has identified optimal substitution patterns for residues that form strands in an antiparallel β-peptide sheet (Krauthauser et al. J. Am. Chem. Soc. 1997, 119, 11719), and we have shown that a dinipecotic acid segment can promote sheet-type interactions between attached strand residues (Chung et al. J. Am. Chem. Soc. 1998, 120, 10555). Here we compare all four possible configurations of the dinipecotic acid segment, (R,S), (S,R), (R,R) and (S,S), for the ability to induce sheet formation with a constant set of enantiomerically pure strand residues. We show that both heterochiral dinipecotic acid segments promote hairpin formation, although one is distinctly superior. Neither of the homochiral dinipecotic acid supports hairpin folding. When the strand residues are β-alanine (achiral), the heterochiral dinipecotic acid segment is again superior to the homochiral segment, but we find a difference between hairpin conformations in solution and in the solid state.
