128135-31-9Relevant academic research and scientific papers
CASPASE INHIBITORS AND METHODS OF USE THEREOF
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Paragraph 00264-00266; 00286-00288, (2020/09/19)
Provided herein are compounds of formula (I), compositions comprising the compounds and method of treating various diseases with the compounds and compositions.
FOLDAMER HELIX BUNDLE-BASED MOLECULAR ENCAPSULATION
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Paragraph 00316; 00317, (2017/03/21)
The present description provides compositions and methods for producing therapeutic oligomeric compounds. In another aspect the description provides methods for administering the oligomeric compounds for the treatment and prevention of disease in a mammal
QUATERNARY ASSEMBLIES OF WATER-SOLUBLE NON-PEPTIDE HELICAL FOLDAMERS, THEIR USE AND PRODUCTION THEREOF
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Paragraph 281; 282, (2017/03/21)
The present description provides compositions and methods for producing therapeutic oligomeric compounds. In another aspect the description provides methods for administering the oligomeric compounds for the treatment and prevention of disease in a mammal
Continuous flow synthesis of β-amino acids from α-amino acids via Arndt-Eistert homologation
Pinho, Vagner D.,Gutmann, Bernhard,Kappe, C. Oliver
, p. 37419 - 37422 (2014/12/09)
A fully continuous four step process for the preparation of β-amino acids from their corresponding α-amino acids utilizing the Arndt-Eistert homologation approach is described. the Partner Organisations 2014.
Synthesis of N-urethane protected α-aminoalkyl-α-cyanomethyl ketones; Application to the synthesis of 3-substituted 5-amino-1H-pyrazole tethered peptidomimetics
Sharnabai,Nagendra,Sureshbabu, Vommina V.
scheme or table, p. 1913 - 1918 (2012/09/25)
The preparation of N-protected amino/peptide α-cyanomethyl ketones through cyanation of the corresponding α-bromomethyl ketones is described. The utility of the resulting α-cyanomethyl ketones in the synthesis of 3-substituted-5-amino-1H-pyrazoles has also been demonstrated. In both steps a wide range of N-protected amino/peptide acids has been employed and the products are obtained in good yield. The enantiomeric purity of both the α-cyanomethyl ketones and pyrazoles were confirmed by chiral HPLC analysis of the corresponding Z-protected d- and l-Ala-OH as model substrates. The synthesis of peptide pyrazolecarboxamides is also delineated. Georg Thieme Verlag Stuttgart · New York.
CuI-promoted one-pot synthesis of N-boc protected β-ketotriazole amino acids: Application in the synthesis of new class of dipeptidomimetics
Vishwanathaa,Narendra,Sureshbabu, Vommina V.
, p. 308 - 314 (2012/07/17)
One-pot click chemistry of Nα-Boc-bromomethylketones, NaN3 and propiolic acid affords N-Boc protected 1,4- disubstituted 1,2,3-β-ketotriazole acids in good to excellent yield. The use of CuI as catalyst and DMSO as solvent leads the click react
Synthesis of optically active β-amino acid N-carboxyanhydrides
Cheng, Jianjun,Ziller, Joseph W.,Deming, Timothy J.
, p. 1943 - 1946 (2007/10/03)
(Equation presented) Methodology has been developed for the general synthesis of optically active β-amino acid N-carboxyanhydrides (β-NCAs) through cyclization of Nβ-Boc or Nβ-Cbz β-amino acids using phosphorus tribromide. The format
Linear and cyclic β3-oligopeptides with functionalised side-chains (-CH2OBn, -CO2Bn, -CH2CH2CO2Bn) derived from serine and from aspartic and glutamic acid
Matthews, Jennifer L.,Gademann, Karl,Jaun, Bernhard,Seebach, Dieter
, p. 3331 - 3340 (2007/10/03)
The natural β-amino acid derivative Boc-Asp(β-OH)-OBn, as well as Boc-β-HGlu(OBn)-OH and Boc-β-HSer(OBn)-OH (prepared from appropriately protected glutamic acid and serine, respectively, by Arndt-Eistert homologation), were employed as building blocks for the synthesis of linear (11-20) and cyclic (21-23) β-oligopeptides consisting of two to six β-amino acids [using trichloroethyl (TCE) ester groups for C-terminal protection and pentafluorophenyl-ester activation for macrocyclisation]. While the linear derivatives are soluble enough for reactions and structural investigations in solution, the cyclo-β-tri- and -hexapeptides are not (according to FT-IR measurements they form networks of hydrogen bonds, perhaps consisting of so-called nanotubes). The CD spectra of the Boc-OTCE-protected (19) and of the unprotected (20) β-hexapeptides [β-Asp(OBn)-β-HGlu(OBn)-β-HSer(OBn)]2 differ drastically, and only the unprotected form shows the familiar pattern of a negative Cotton effect between 210 and 220 nm (indicative of a 314 helix). An NMR analysis in methanol of the β-hexapeptide 20 with free termini reveals the presence of a single, central, left-handed helix turn (14-membered hydrogen-bonded ring). The results are discussed and compared with those obtained previously for analogous β-peptides carrying non-functionalised side chains.
Synthesis of acyclic and dehydroaspartic acid analogues of Ac-Asp-Glu-OH and their inhibition of rat brain N-acetylated α-linked acidic dipeptidase (NAALA dipeptidase)
Subasinghe,Schulte,Chan,Roon,Koerner,Johnson
, p. 2734 - 2744 (2007/10/02)
The following structural and conformationally constrained analogues of Ac-Asp-Glu-OH (1) were synthesized: Ac-Glu-Glu-OH (2), Ac-D-Asp-Glu-OH (3), Ac-Glu-Asp-OH (4), Ac-Asp-Asp-OH (5), Ac-Asp-3-aminohexanedioic acid (6), Ac-3-amino-3-(carboxymethyl)propanoyl-Glu-OH (7), N-succinyl-Glu-OH (8), N-maleyl-Glu-OH (9), N-fumaryl-Glu-OH (10), and Ac-Δ(z)Asp-Glu-OH (11). These analogues were evaluated for their ability to inhibit the hydrolysis of Ac-Asp-[3,4-3H]-Glu-OH by N-acetylated α-linked acidic dipeptidase (NAALA dipeptidase) in order to gain some insight into the structural requirements for the inhibition of this enzyme. Analogues 4-6 and 9 were very weak inhibitors of NAALA dipeptidase (K(i) > 40 μM), while 2, 3, and 7 with K(i) values ranging from 3.2-8.5 μM showed intermediate inhibitory activity. The most active inhibitors of NAALA dipeptidase were compounds 8, 10, and 11 with K(i) values of 0.9, 0.4, and 1.4 μM, respectively. These results suggest that the relative spacing between the side chain carboxyl and the α-carboxyl group of the C-terminal residue may be important for binding to the active site of the enzyme. They also indicate that the χ1 torsional angle for the aspartyl residue is in the vicinity of 0°.
