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Volumn 48, Issue 24, 2005, Pages 7623-7627

Preorganization of the hydroxyethylene dipeptide isostere: The preferred conformation in solution resembles the conformation bound to BACE

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC PROTEINASE; BETA SECRETASE; BETA SECRETASE INHIBITOR; HYDROXYETHYLENE DIPEPTIDE ISOSTERE; UNCLASSIFIED DRUG;

EID: 28144436378     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm050631+     Document Type: Article
Times cited : (8)

References (30)
  • 1
    • 0036218648 scopus 로고    scopus 로고
    • Aspartic proteinases in disease: A structural perspective
    • Cooper, J. B. Aspartic Proteinases in Disease: a Structural Perspective. Curr. Drug Targets 2002, 3, 155-173.
    • (2002) Curr. Drug Targets , vol.3 , pp. 155-173
    • Cooper, J.B.1
  • 2
    • 0026005186 scopus 로고
    • Human immunodeficiency virus-1 protease. 2. Use of pH rate studies and solvent kinetic isotope effects to elucidate details of chemical mechanism
    • Hyland, L. J.; Tomaszek, T. A., Jr.; Meek, T. D. Human Immunodeficiency Virus-1 Protease. 2. Use of pH Rate Studies and Solvent Kinetic Isotope Effects to Elucidate Details of Chemical Mechanism. Biochemistry 1991, 30, 8454-8463.
    • (1991) Biochemistry , vol.30 , pp. 8454-8463
    • Hyland, L.J.1    Tomaszek Jr., T.A.2    Meek, T.D.3
  • 4
    • 0002170421 scopus 로고
    • Chemistry of renin inhibitors
    • Kostka, V., Eds.; de Gruyter: Berlin, Germany
    • Szelke, M. Chemistry of Renin Inhibitors. In Aspartic Proteinases and their Inhibitors; Kostka, V., Eds.; de Gruyter: Berlin, Germany, 1985; pp 421-441.
    • (1985) Aspartic Proteinases and Their Inhibitors , pp. 421-441
    • Szelke, M.1
  • 5
    • 0034042866 scopus 로고    scopus 로고
    • Approaches to the design of effective HIV-1 protease inhibitors
    • Lebon, F.; Ledecq, M. Approaches to the Design of Effective HIV-1 Protease Inhibitors. Curr. Med. Chem. 2000, 7, 455-477.
    • (2000) Curr. Med. Chem. , vol.7 , pp. 455-477
    • Lebon, F.1    Ledecq, M.2
  • 8
    • 17244364283 scopus 로고    scopus 로고
    • Proteases universally recognize beta strands in their active sites
    • Tyndall, J. D. A.; Nall, T.; Fairlie, D. P. Proteases Universally Recognize Beta Strands in Their Active Sites. Chem. Rev. 2005, 105, 973-999.
    • (2005) Chem. Rev. , vol.105 , pp. 973-999
    • Tyndall, J.D.A.1    Nall, T.2    Fairlie, D.P.3
  • 10
    • 0026640040 scopus 로고
    • Flexible molecules with defined shape-conformational design
    • Hoffmann, R. W. Flexible Molecules with Defined Shape-Conformational Design. Angew. Chem., Int. Ed. Engl. 1992, 31, 1124-1134.
    • (1992) Angew. Chem., Int. Ed. Engl. , vol.31 , pp. 1124-1134
    • Hoffmann, R.W.1
  • 11
    • 0034674252 scopus 로고    scopus 로고
    • Conformational design of open-chain compounds
    • Hoffmann, R. W. Conformational Design of Open-Chain Compounds. Angew. Chem., Int. Ed. 2000, 39, 2054-2070.
    • (2000) Angew. Chem., Int. Ed. , vol.39 , pp. 2054-2070
    • Hoffmann, R.W.1
  • 12
    • 0036964237 scopus 로고    scopus 로고
    • Designed beta-turn mimic based on the allylic-strain concept: Evaluation of structural and biological features by incorporation into cyclic RGD peptide (Cyclo(-L-arginylglycyl-L-α-aspartyl-))
    • Sukopp, M.; Marinelli, L.; Heller, M.; Brandi, T.; Goodman, S. L.; Hoffman, R. W.; Kessler, H. Designed Beta-Turn Mimic Based on the Allylic-Strain Concept: Evaluation of Structural and Biological Features by Incorporation into Cyclic RGD Peptide (Cyclo(-L-arginylglycyl-L-α-aspartyl-)). Helv. Chim. Acta 2002, 85, 4442-4452.
    • (2002) Helv. Chim. Acta , vol.85 , pp. 4442-4452
    • Sukopp, M.1    Marinelli, L.2    Heller, M.3    Brandi, T.4    Goodman, S.L.5    Hoffman, R.W.6    Kessler, H.7
  • 16
    • 20444483055 scopus 로고
    • The relationship between proton-proton NMR coupling constants and substituent electronegativities-I
    • Haasnot, C. A. G.; de Leeuw, F. A. A. M.; Altona C. The Relationship between Proton-Proton NMR Coupling Constants and Substituent Electronegativities-I. Tetrahedron 1980, 36, 2783-2792.
    • (1980) Tetrahedron , vol.36 , pp. 2783-2792
    • Haasnot, C.A.G.1    De Leeuw, F.A.A.M.2    Altona, C.3
  • 17
    • 0008560922 scopus 로고    scopus 로고
    • Conformational analysis of peptides: Application to drug design
    • Craik, D. J., Eds.; CRC Press: Boca Raton, FL
    • Kessler, H.; Konat, R. K.; Schmitt, W. Conformational Analysis of Peptides: Application to Drug Design. In NMR in Drug Design; Craik, D. J., Eds.; CRC Press: Boca Raton, FL, 1996; pp 215-244.
    • (1996) NMR in Drug Design , pp. 215-244
    • Kessler, H.1    Konat, R.K.2    Schmitt, W.3
  • 18
    • 0037571112 scopus 로고    scopus 로고
    • Merck molecular force field. I. Basis, form, scope, parametrization, and performance of MMFF94
    • Halgren, T. A. Merck Molecular Force Field. I. Basis, Form, Scope, Parametrization, and Performance of MMFF94. J. Comput. Chem. 1996, 17, 490-519.
    • (1996) J. Comput. Chem. , vol.17 , pp. 490-519
    • Halgren, T.A.1
  • 19
    • 0347991962 scopus 로고    scopus 로고
    • NMR structural characterization of peptide inhibitors bound to the hepatitis C virus NS3 protease: Design of a new P2 substituent
    • Goudreau, N.; Cameron, D. R.; Bonneau, P.; Gorys, V.; Plouffe, C.; Poirier, M.; Lamarre, D.; Llinas-Brunet, M. NMR Structural Characterization of Peptide Inhibitors Bound to the Hepatitis C Virus NS3 Protease: Design of a New P2 Substituent. J. Med. Chem. 2004, 47, 123-132.
    • (2004) J. Med. Chem. , vol.47 , pp. 123-132
    • Goudreau, N.1    Cameron, D.R.2    Bonneau, P.3    Gorys, V.4    Plouffe, C.5    Poirier, M.6    Lamarre, D.7    Llinas-Brunet, M.8
  • 21
    • 0029978353 scopus 로고    scopus 로고
    • Analysis of main chain torsion angles in proteins: Prediction of NMR coupling constants for native and random coil conformations
    • Smith, L. J.; Bolin K. A.; Schwalbe, H.; MacArthur, M. W.; Thornton, J. M.; Dobson, C. M. Analysis of Main Chain Torsion Angles in Proteins: Prediction of NMR Coupling Constants for Native and Random Coil Conformations. J. Mol. Biol. 1996, 255, 494-506.
    • (1996) J. Mol. Biol. , vol.255 , pp. 494-506
    • Smith, L.J.1    Bolin, K.A.2    Schwalbe, H.3    MacArthur, M.W.4    Thornton, J.M.5    Dobson, C.M.6
  • 22
    • 0000749460 scopus 로고    scopus 로고
    • Toward a description of the conformations of denatured states of proteins. Comparison of a random coil model with NMR measurements
    • Fiebig, K. M.; Schwalbe, H.; Buck, M.; Smith, L. J.; Dobson, C. M. Toward a Description of the Conformations of Denatured States of Proteins. Comparison of a Random Coil Model with NMR Measurements. J. Phys. Chem. 1996, 100, 2661-2666.
    • (1996) J. Phys. Chem. , vol.100 , pp. 2661-2666
    • Fiebig, K.M.1    Schwalbe, H.2    Buck, M.3    Smith, L.J.4    Dobson, C.M.5
  • 23
  • 24
    • 0034929804 scopus 로고    scopus 로고
    • Macrocycles mimic the extended peptide conformation recognized by aspartic, serine, cysteine and metallo proteases
    • Tyndall, J. D. A.; Fairlie, D. P. Macrocycles Mimic the Extended Peptide Conformation Recognized By Aspartic, Serine, Cysteine and Metallo Proteases. Curr. Med. Chem. 2001, 8, 893-907.
    • (2001) Curr. Med. Chem. , vol.8 , pp. 893-907
    • Tyndall, J.D.A.1    Fairlie, D.P.2
  • 30
    • 3843138591 scopus 로고    scopus 로고
    • Stereoselective synthesis of constrained oxacyclic hydroxyethylene isosteres of aspartyl protease inhibitors. Nitroaldol methodology toward 2,3-substituted tetrahydrofurans
    • Hanessian, S.; Brassard, M. Stereoselective Synthesis of Constrained Oxacyclic Hydroxyethylene Isosteres of Aspartyl Protease Inhibitors. Nitroaldol Methodology toward 2,3-Substituted Tetrahydrofurans. Tetrahedron 2004, 60, 7621-7628.
    • (2004) Tetrahedron , vol.60 , pp. 7621-7628
    • Hanessian, S.1    Brassard, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.