메뉴 건너뛰기




Volumn 5, Issue 9, 2014, Pages 1037-1042

C-terminal residue optimization and fragment merging: Discovery of a potent peptide-hybrid inhibitor of dengue protease

Author keywords

Dengue virus; fragment merging; peptide; protease inhibitor

Indexed keywords

2,4 THIAZOLIDINEDIONE DERIVATIVE; AMINO ACID DERIVATIVE; NORLEUCINE; PEPTIDE; PEPTIDE DERIVATIVE; PHENYLGLYCINE; PIPECOLIC ACID; PROTEINASE; PROTEINASE INHIBITOR;

EID: 84907569335     PISSN: None     EISSN: 19485875     Source Type: Journal    
DOI: 10.1021/ml500245v     Document Type: Article
Times cited : (56)

References (36)
  • 2
    • 84877269372 scopus 로고    scopus 로고
    • Dengue more prevalent than previously thought
    • Mitka, M. Dengue more prevalent than previously thought JAMA 2013, 309 (18) 1882-1882
    • (2013) JAMA , vol.309 , Issue.18 , pp. 1882-1882
    • Mitka, M.1
  • 3
    • 84882824658 scopus 로고    scopus 로고
    • The invasive mosquito species Aedes albopictus: Current knowledge and future perspectives
    • Bonizzoni, M.; Gasperi, G.; Chen, X.; James, A. A. The invasive mosquito species Aedes albopictus: current knowledge and future perspectives Trends Parasitol. 2013, 29 (9) 460-468
    • (2013) Trends Parasitol. , vol.29 , Issue.9 , pp. 460-468
    • Bonizzoni, M.1    Gasperi, G.2    Chen, X.3    James, A.A.4
  • 4
    • 84880810570 scopus 로고    scopus 로고
    • Viral proteases as targets for drug design
    • Skorenski, M.; Sienczyk, M. Viral proteases as targets for drug design Curr. Pharm. Des. 2013, 19 (6) 1126-53
    • (2013) Curr. Pharm. Des. , vol.19 , Issue.6 , pp. 1126-1153
    • Skorenski, M.1    Sienczyk, M.2
  • 5
    • 84890947330 scopus 로고    scopus 로고
    • Novel Therapeutic Approaches for Hepatitis C
    • Au, J. S.; Pockros, P. J. Novel Therapeutic Approaches for Hepatitis C Clin. Pharmacol. Ther. 2014, 95 (1) 78-88
    • (2014) Clin. Pharmacol. Ther. , vol.95 , Issue.1 , pp. 78-88
    • Au, J.S.1    Pockros, P.J.2
  • 6
    • 61449189645 scopus 로고    scopus 로고
    • Anti-HIV drugs: 25 compounds approved within 25 years after the discovery of HIV
    • De Clercq, E. Anti-HIV drugs: 25 compounds approved within 25 years after the discovery of HIV Int. J. Antimicrob. Agents 2009, 33 (4) 307-320
    • (2009) Int. J. Antimicrob. Agents , vol.33 , Issue.4 , pp. 307-320
    • De Clercq, E.1
  • 7
    • 53249121029 scopus 로고    scopus 로고
    • Towards the design of antiviral inhibitors against flaviviruses: The case for the multifunctional NS3 protein from Dengue virus as a target
    • Lescar, J.; Luo, D.; Xu, T.; Sampath, A.; Lim, S. P.; Canard, B.; Vasudevan, S. G. Towards the design of antiviral inhibitors against flaviviruses: The case for the multifunctional NS3 protein from Dengue virus as a target Antiviral Res. 2008, 80 (2) 94-101
    • (2008) Antiviral Res. , vol.80 , Issue.2 , pp. 94-101
    • Lescar, J.1    Luo, D.2    Xu, T.3    Sampath, A.4    Lim, S.P.5    Canard, B.6    Vasudevan, S.G.7
  • 8
    • 0031975823 scopus 로고    scopus 로고
    • Mutagenesis of the NS3 protease of Dengue virus type 2
    • Valle, R. P. C.; Falgout, B. Mutagenesis of the NS3 protease of Dengue virus type 2 J. Virol. 1998, 72 (1) 624-632
    • (1998) J. Virol. , vol.72 , Issue.1 , pp. 624-632
    • Valle, R.P.C.1    Falgout, B.2
  • 9
    • 0025864149 scopus 로고
    • Both nonstructural proteins NS2B and NS3 are required for the proteolytic processing of dengue virus nonstructural proteins
    • Falgout, B.; Pethel, M.; Zhang, Y. M.; Lai, C. J. Both nonstructural proteins NS2B and NS3 are required for the proteolytic processing of dengue virus nonstructural proteins J. Virol. 1991, 65 (5) 2467-2475
    • (1991) J. Virol. , vol.65 , Issue.5 , pp. 2467-2475
    • Falgout, B.1    Pethel, M.2    Zhang, Y.M.3    Lai, C.J.4
  • 11
    • 84871380932 scopus 로고    scopus 로고
    • Characterization of 8-hydroxyquinoline derivatives containing aminobenzothiazole as inhibitors of dengue virus type 2 protease in vitro
    • Lai, H.; Sridhar Prasad, G.; Padmanabhan, R. Characterization of 8-hydroxyquinoline derivatives containing aminobenzothiazole as inhibitors of dengue virus type 2 protease in vitro Antiviral Res. 2013, 97 (1) 74-80
    • (2013) Antiviral Res. , vol.97 , Issue.1 , pp. 74-80
    • Lai, H.1    Sridhar Prasad, G.2    Padmanabhan, R.3
  • 12
    • 84856213045 scopus 로고    scopus 로고
    • Inhibition of Dengue virus and West Nile virus proteases by click chemistry-derived benz[ d ]isothiazol-3(2 H)-one derivatives
    • Tiew, K. C.; Dou, D.; Teramoto, T.; Lai, H.; Alliston, K. R.; Lushington, G. H.; Padmanabhan, R.; Groutas, W. C. Inhibition of Dengue virus and West Nile virus proteases by click chemistry-derived benz[ d ]isothiazol-3(2 H)-one derivatives Bioorg. Med. Chem. 2012, 20 (3) 1213-1221
    • (2012) Bioorg. Med. Chem. , vol.20 , Issue.3 , pp. 1213-1221
    • Tiew, K.C.1    Dou, D.2    Teramoto, T.3    Lai, H.4    Alliston, K.R.5    Lushington, G.H.6    Padmanabhan, R.7    Groutas, W.C.8
  • 13
    • 78751620005 scopus 로고    scopus 로고
    • Anthracene-based inhibitors of dengue virus NS2B-NS3 protease
    • Tomlinson, S. M.; Watowich, S. J. Anthracene-based inhibitors of dengue virus NS2B-NS3 protease Antiviral Res. 2011, 89 (2) 127-135
    • (2011) Antiviral Res. , vol.89 , Issue.2 , pp. 127-135
    • Tomlinson, S.M.1    Watowich, S.J.2
  • 14
    • 0035824539 scopus 로고    scopus 로고
    • Activity of recombinant Dengue 2 virus NS3 protease in the presence of a truncated NS2B co-factor, small peptide substrates, and inhibitors
    • Leung, D.; Schroder, K.; White, H.; Fang, N. X.; Stoermer, M. J.; Abbenante, G.; Martin, J. L.; Young, P. R.; Fairlie, D. P. Activity of recombinant Dengue 2 virus NS3 protease in the presence of a truncated NS2B co-factor, small peptide substrates, and inhibitors J. Biol. Chem. 2001, 276 (49) 45762-45771
    • (2001) J. Biol. Chem. , vol.276 , Issue.49 , pp. 45762-45771
    • Leung, D.1    Schroder, K.2    White, H.3    Fang, N.X.4    Stoermer, M.J.5    Abbenante, G.6    Martin, J.L.7    Young, P.R.8    Fairlie, D.P.9
  • 20
    • 0034616194 scopus 로고    scopus 로고
    • Purified NS2B/NS3 serine protease of Dengue virus type 2 exhibits cofactor NS2B dependence for cleavage of substrates with dibasic amino acids in vitro
    • Yusof, R.; Clum, S.; Wetzel, M.; Murthy, H. M. K.; Padmanabhan, R. Purified NS2B/NS3 serine protease of Dengue virus type 2 exhibits cofactor NS2B dependence for cleavage of substrates with dibasic amino acids in vitro J. Biol. Chem. 2000, 275 (14) 9963-9969
    • (2000) J. Biol. Chem. , vol.275 , Issue.14 , pp. 9963-9969
    • Yusof, R.1    Clum, S.2    Wetzel, M.3    Murthy, H.M.K.4    Padmanabhan, R.5
  • 22
    • 84858145412 scopus 로고    scopus 로고
    • Retro peptide-hybrids as selective inhibitors of the Dengue virus NS2B-NS3 protease
    • Nitsche, C.; Behnam, M. A. M.; Steuer, C.; Klein, C. D. Retro peptide-hybrids as selective inhibitors of the Dengue virus NS2B-NS3 protease Antiviral Res. 2012, 94 (1) 72-79
    • (2012) Antiviral Res. , vol.94 , Issue.1 , pp. 72-79
    • Nitsche, C.1    Behnam, M.A.M.2    Steuer, C.3    Klein, C.D.4
  • 23
    • 84887869847 scopus 로고    scopus 로고
    • Thiazolidinone-peptide hybrids as Dengue virus protease inhibitors with antiviral activity in cell culture
    • Nitsche, C.; Schreier, V. N.; Behnam, M. A. M.; Kumar, A.; Bartenschlager, R.; Klein, C. D. Thiazolidinone-peptide hybrids as Dengue virus protease inhibitors with antiviral activity in cell culture J. Med. Chem. 2013, 56 (21) 8389-8403
    • (2013) J. Med. Chem. , vol.56 , Issue.21 , pp. 8389-8403
    • Nitsche, C.1    Schreier, V.N.2    Behnam, M.A.M.3    Kumar, A.4    Bartenschlager, R.5    Klein, C.D.6
  • 24
    • 84880122957 scopus 로고    scopus 로고
    • Fluorimetric and HPLC-Based Dengue Virus Protease Assays Using a FRET Substrate
    • Gong, E. Y. Humana Press: New York
    • Nitsche, C.; Klein, C. Fluorimetric and HPLC-Based Dengue Virus Protease Assays Using a FRET Substrate. In Antiviral Methods and Protocols; Gong, E. Y., Ed.; Humana Press: New York, 2013; Vol. 1030, pp 221-236.
    • (2013) Antiviral Methods and Protocols , vol.1030 , pp. 221-236
    • Nitsche, C.1    Klein, C.2
  • 25
    • 0025116324 scopus 로고
    • Flavivirus genome organization, expression, and replication
    • Chambers, T. J.; Hahn, C. S.; Galler, R.; Rice, C. M. Flavivirus genome organization, expression, and replication Annu. Rev. Microbiol. 1990, 44 (1) 649-688
    • (1990) Annu. Rev. Microbiol. , vol.44 , Issue.1 , pp. 649-688
    • Chambers, T.J.1    Hahn, C.S.2    Galler, R.3    Rice, C.M.4
  • 27
    • 33847381100 scopus 로고    scopus 로고
    • A decade of fragment-based drug design: Strategic advances and lessons learned
    • Hajduk, P. J.; Greer, J. A decade of fragment-based drug design: strategic advances and lessons learned Nat. Rev. Drug Discovery 2007, 6 (3) 211-219
    • (2007) Nat. Rev. Drug Discovery , vol.6 , Issue.3 , pp. 211-219
    • Hajduk, P.J.1    Greer, J.2
  • 28
    • 33751204422 scopus 로고    scopus 로고
    • Fragment-based lead discovery: A chemical update
    • Erlanson, D. A. Fragment-based lead discovery: A chemical update Curr. Opin. Biotechnol. 2006, 17 (6) 643-652
    • (2006) Curr. Opin. Biotechnol. , vol.17 , Issue.6 , pp. 643-652
    • Erlanson, D.A.1
  • 29
    • 82255192015 scopus 로고    scopus 로고
    • Arylcyanoacrylamides as inhibitors of the Dengue and West Nile virus proteases
    • Nitsche, C.; Steuer, C.; Klein, C. D. Arylcyanoacrylamides as inhibitors of the Dengue and West Nile virus proteases Bioorg. Med. Chem. 2011, 19 (24) 7318-7337
    • (2011) Bioorg. Med. Chem. , vol.19 , Issue.24 , pp. 7318-7337
    • Nitsche, C.1    Steuer, C.2    Klein, C.D.3
  • 30
    • 77950571108 scopus 로고    scopus 로고
    • New substructure filters for removal of pan assay interference compounds (PAINS) from screening libraries and for their exclusion in bioassays
    • Baell, J. B.; Holloway, G. A. New substructure filters for removal of pan assay interference compounds (PAINS) from screening libraries and for their exclusion in bioassays J. Med. Chem. 2010, 53 (7) 2719-2740
    • (2010) J. Med. Chem. , vol.53 , Issue.7 , pp. 2719-2740
    • Baell, J.B.1    Holloway, G.A.2
  • 31
    • 84856383832 scopus 로고    scopus 로고
    • Privileged scaffolds or promiscuous binders: A comparative study on rhodanines and related heterocycles in medicinal chemistry
    • Mendgen, T.; Steuer, C.; Klein, C. D. Privileged scaffolds or promiscuous binders: A comparative study on rhodanines and related heterocycles in medicinal chemistry J. Med. Chem. 2011, 55 (2) 743-753
    • (2011) J. Med. Chem. , vol.55 , Issue.2 , pp. 743-753
    • Mendgen, T.1    Steuer, C.2    Klein, C.D.3
  • 33
    • 84855921187 scopus 로고    scopus 로고
    • Ligand-bound structures of the Dengue virus protease reveal the active conformation
    • Noble, C. G.; Seh, C. C.; Chao, A. T.; Shi, P. Y. Ligand-bound structures of the Dengue virus protease reveal the active conformation J. Virol. 2012, 86 (1) 438-446
    • (2012) J. Virol. , vol.86 , Issue.1 , pp. 438-446
    • Noble, C.G.1    Seh, C.C.2    Chao, A.T.3    Shi, P.Y.4
  • 34
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
    • Trott, O.; Olson, A. J. AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading J. Comput. Chem. 2010, 31 (2) 455-461
    • (2010) J. Comput. Chem. , vol.31 , Issue.2 , pp. 455-461
    • Trott, O.1    Olson, A.J.2
  • 35
    • 0035964342 scopus 로고    scopus 로고
    • Electrostatics of nanosystems: Application to microtubules and the ribosome
    • Baker, N. A.; Sept, D.; Joseph, S.; Holst, M. J.; McCammon, J. A. Electrostatics of nanosystems: Application to microtubules and the ribosome Proc. Natl. Acad. Sci. U.S.A. 2001, 98 (18) 10037-10041
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , Issue.18 , pp. 10037-10041
    • Baker, N.A.1    Sept, D.2    Joseph, S.3    Holst, M.J.4    McCammon, J.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.