209173-80-8Relevant academic research and scientific papers
COMPOSITION FOR TREATMENT AND/OR PREVENTION OF PERIPHERAL NERVE DISORDER
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Paragraph 0186, (2019/10/29)
The present invention provides a means for treating and/or preventing peripheral nerve disorder by facilitating regeneration of peripheral nerves. Specifically, the present invention provides a composition for treating and/or preventing peripheral nerve d
Lissencephaly therapeutic agent
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Page/Page column 35, (2016/07/27)
An object of the present invention is to provide a medicament and method for treating lissencephaly patients. The present invention provides a lissencephaly therapeutic or preventive agent comprising a compound represented by the general formula (I): wher
LISSENCEPHALY THERAPEUTIC AGENT
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Page/Page column, (2013/10/22)
An object of the present invention is to provide a medicament and method for treating lissencephaly patients. The present invention provides a lissencephaly therapeutic or preventive agent comprising a compound represented by the general formula (I): wher
Exploration of orally available calpain inhibitors: Peptidyl α-ketoamides containing an amphiphile at P3 site
Shirasaki, Yoshihisa,Miyashita, Hiroyuki,Yamaguchi, Masazumi,Inoue, Jun,Nakamura, Masayuki
, p. 4473 - 4484 (2007/10/03)
A novel series of dipeptidyl α-ketoamide derivatives with amphiphile was designed and synthesized as water-soluble calpain inhibitors. The introduction of amphiphiles at the P3 site increased water solubility without loss of membrane permeability and prov
ALPHA-KETOAMIDE DERIVATIVE, AND PRODUCTION METHOD AND USE THEREOF
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Page/Page column 33, (2008/06/13)
The present invention provides a compound represented by the formula (I): (INSERT CHEMICAL FORMULA) (wherein R1 is a lower alkyl substituted by a lower alkoxy or a heterocyclic group, or a heterocyclic group; R2 is a lower alkyl opti
Design, Synthesis, Molecular Modeling Studies, and Calpain Inhibitory Activity of Novel α-Ketoamides Incorporating Polar Residues at the P 1′-Position
Donkor, Isaac O.,Han, Jie,Zheng, Xiaozhang
, p. 72 - 79 (2007/10/03)
A series of novel α-ketoamides incorporating stereoisomeric residues with different electronic properties at the P1′-position were synthesized to study the electronic requirements for inhibitor binding to the S1′-subsite of calpain I
Significance of hydrogen bonding at the S1′ subsite of calpain I
Donkor, Isaac O.,Zheng, Xiaozhang,Han, Jie,Lacy, Calvin,Miller, Duane D.
, p. 1753 - 1755 (2007/10/03)
α-Ketohydroxamates were synthesized as bioisosteres of α-ketoamides. The α-ketohydroxamates were generally more potent than the corresponding α-ketoamides. The potency of the compounds suggests that hydrogen bonding and steric bulk of substituents on the nitrogen atom of the ketoamide moiety influence calpain inhibition.
Synthesis of di- and tripeptide analogues containing α-ketoamide as a new core structure for inhibition of HIV-1 protease
Sheha, Mahmoud M.,Mahfouz, Nadia M.,Hassan, Hoda Y.,Youssef, Adel F.,Mimoto, Tsutomu,Kiso, Yoshiaki
, p. 887 - 894 (2007/10/03)
Di- and tripeptide analogues containing α-ketoamide as a new core structure and incorporating allophenylnorstatine (Apns) as a transition state mimic, were designed and synthesized in the hope of obtaining a novel structural type of HIV-1 protease inhibitors. The immediate precursor, Apns-Thz-NHBu(t) was prepared by coupling of Boc-Apns with N-tert·butyl Thz-4-carboxamide hydrochloride. Removal of Boc group followed by coupling with the respective α-ketoacid residue (P2) gave the desired dipeptides (8-12) in almost quantitative yields. The α-keto tripeptides (18-21) were obtained by oxidation of the hydroxyl group of Apns (PI) in the appropriate tripeptide, iQOA-Val-Apns-(un)substituted Thz(Oxa)-NHBu1 with DMSO/DCC. Preliminary evaluation of the activity of the synthesized derivatives was determined as percentage of enzyme inhibition at 5 μM and 50 nM levels of the di- and tripeptides respectively. The α-ketoamides displayed a significant enhanced potency relative to their parent isosteres as inhibitors of HIV-1 protease and are shown to be a promising new core structure for the development of enzyme inhibitors. A quantitative approach was attempted, using an LFE model, correlating the effect of structural modification and HIV-1 protease inhibition activity of the prepared dipeptides. The result indicates the contribution of the torsion angle by 84% to the activity of the inhibitors. (C) 2000 Editions scientifiques et medicales Elsevier SAS.
Synthesis and calpain inhibitory activity of α-ketoamides with 2,3-methanoleucine stereoisomers at the P2 position
Donkor, Isaac O.,Zheng, Xiaozhang,Miller, Duane D.
, p. 2497 - 2500 (2007/10/03)
A series of novel ketoamides incorporating all four 2,3-methanoleucine stereoisomers at the P2 position was synthesized. The compounds displayed a wide variation in K(i) values for inhibition of calpain I depending on the configuration of the P
Process for preparing beta -amino- alpha -hydroxy acid derivatives
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, (2008/06/13)
PCT No. PCT/JP97/02844 Sec. 371 Date May 14, 1999 Sec. 102(e) Date May 14, 1999 PCT Filed Aug. 18, 1997 PCT Pub. No. WO98/07687 PCT Pub. Date Feb. 26, 1998An object of the present invention is to provide a process for producing a beta -amino- alpha -hydro
