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Volumn 21, Issue 7, 2014, Pages 646-656

In silico molecular interaction analysis of ltnf peptide-lt10 with snake venom enzymes

Author keywords

Atrolysin C; LT10; LTNF; PLA2; Snake envenomation; Toxin neutralization

Indexed keywords

ATROLYSIN C; ENZYME; LETHAL TOXIN NEUTRALIZING FACTOR; PEPTIDE DERIVATIVE; PEPTIDE LT10; PROTEIN PLA2; SNAKE VENOM; SNAKE VENOM ENZYME; SYNTHETIC PEPTIDE; UNCLASSIFIED DRUG; METALLOPROTEINASE; PEPTIDE FRAGMENT; RECOMBINANT PROTEIN; VENOM ANTISERUM;

EID: 84901920320     PISSN: 09298665     EISSN: 18755305     Source Type: Journal    
DOI: 10.2174/0929866521666140320112142     Document Type: Article
Times cited : (5)

References (47)
  • 1
    • 0024505685 scopus 로고
    • Snake envenomation. Incidence, clinical presentation and management
    • Nelson, B.K. Snake envenomation. Incidence, clinical presentation and management. Med. Toxicol. Adverse Drug Exp., 1989, 4, 17-31.
    • (1989) Med. Toxicol. Adverse Drug Exp. , vol.4 , pp. 17-31
    • Nelson, B.K.1
  • 2
    • 33846105870 scopus 로고    scopus 로고
    • Snake venom components and their applications in biomedicine
    • Koh, D.C.; Armugam, A.; Jeyaseelan, K. Snake venom components and their applications in biomedicine. Cell. Mol. Life Sci., 2006, 63, 303041.
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 3030-3041
    • Koh, D.C.1    Armugam, A.2    Jeyaseelan, K.3
  • 3
    • 78349297916 scopus 로고    scopus 로고
    • Inhibition of hemorragic snake venom components: Old and new approaches
    • Panfoli, I.; Calzia, D.; Ravera, S.; Morelli, A. Inhibition of hemorragic snake venom components: old and new approaches. Toxins (Basel), 2010, 2, 41727.
    • (2010) Toxins (Basel , vol.2 , pp. 417-427
    • Panfoli, I.1    Calzia, D.2    Ravera, S.3    Morelli, A.4
  • 5
    • 13744256871 scopus 로고    scopus 로고
    • Snake venoms and antivenoms: Critical supply issues
    • Bawaskar, H.S. Snake venoms and antivenoms: critical supply issues. J. Assoc. Physicians India, 2004, 52, 1113.
    • (2004) J. Assoc. Physicians India , vol.52 , pp. 11-13
    • Bawaskar, H.S.1
  • 6
    • 0031803535 scopus 로고    scopus 로고
    • Venoms antivenoms and immunotherapy
    • Chippaux, J.P.; Goyffon, M. Venoms, antivenoms and immunotherapy. Toxicon, 1998, 36, 823846.
    • (1998) Toxicon , vol.36 , pp. 823-846
    • Chippaux, J.P.1    Goyffon, M.2
  • 7
    • 0002145534 scopus 로고    scopus 로고
    • Anti-lethal factor from opossum serum is a potent antidote for animal, plant and bacterial toxins
    • Lipps, B. Anti-lethal factor from opossum serum is a potent antidote for animal, plant and bacterial toxins. J. Venom Anim. Toxins Incl. Trop. Dis., 1999, 5, 5666.
    • (1999) J. Venom Anim. Toxins Incl. Trop. Dis. , vol.5 , pp. 56-66
    • Lipps, B.1
  • 10
    • 0002342276 scopus 로고    scopus 로고
    • Small synthetic peptides inhibit, in mice, the lethalithy of toxins derived from animal, plant and bacteria
    • LIPPS, B. Small synthetic peptides inhibit, in mice, the lethalithy of toxins derived from animal, plant and bacteria. J. Venom Anim. Toxins Incl. Trop. Dis., 2000, 6, 7786.
    • (2000) J. Venom Anim. Toxins Incl. Trop. Dis. , vol.6 , pp. 77-86
    • Lipps, B.1
  • 11
    • 45849129584 scopus 로고    scopus 로고
    • In vitro assay of biological and chemical toxins using antibodies against lethal toxin neutralizing factor
    • Lipps, B. In vitro assay of biological and chemical toxins using antibodies against lethal toxin neutralizing factor. J. Venom Anim. Toxins Incl. Trop. Dis., 2002, 8, 214255.
    • (2002) J. Venom Anim. Toxins Incl. Trop. Dis. , vol.8 , pp. 214-255
    • Lipps, B.1
  • 13
    • 84864452901 scopus 로고    scopus 로고
    • Pep-fold: An updated de novo structure prediction server for both linear and disulfide bonded cyclic peptides
    • Thévenet, P.; Shen, Y.; Maupetit, J.; Guyon, F.; Derreumaux, P.; Tufféry, P. PEP-FOLD: an updated de novo structure prediction server for both linear and disulfide bonded cyclic peptides. Nucleic Acids Res., 2012, 40, W288-W293.
    • (2012) Nucleic Acids Res. , vol.40
    • Thévenet, P.1    Shen, Y.2    Maupetit, J.3    Guyon, F.4    Derreumaux, P.5    Tufféry, P.6
  • 14
    • 67849130555 scopus 로고    scopus 로고
    • Pep-fold: An online resource for de novo peptide structure prediction
    • Maupetit, J.; Derreumaux, P.; Tuffery, P. PEP-FOLD: an online resource for de novo peptide structure prediction. Nucleic Acids Res., 2009, 37, W498-W503.
    • (2009) Nucleic Acids Res. , vol.37
    • Maupetit, J.1    Derreumaux, P.2    Tuffery, P.3
  • 16
    • 79953212647 scopus 로고    scopus 로고
    • Reversescreen3d: A structure-based ligand matching method to identify protein targets
    • Kinnings, S.L.; Jackson, R.M. ReverseScreen3D: a structure-based ligand matching method to identify protein targets. J. Chem. Inf. Model., 2011, 51, 624634.
    • (2011) J. Chem. Inf. Model. , vol.51 , pp. 624-634
    • Kinnings, S.L.1    Jackson, R.M.2
  • 17
    • 1642310340 scopus 로고    scopus 로고
    • Glide: A new approach for rapid, accurate docking and scoring. 2. Enrichment factors in database screening
    • Halgren, T.A.; Murphy, R.B.; Friesner, R.A.; Beard, H. S.; Frye, L.L.; Pollard, W.T.; Banks, J.L. Glide: a new approach for rapid, accurate docking and scoring. 2. Enrichment factors in database screening. J. Med. Chem., 2004, 47, 17501759.
    • (2004) J. Med. Chem. , Issue.47 , pp. 1750-1759
    • Halgren, T.A.1    Murphy, R.B.2    Friesner, R.A.3    Beard, H.S.4    Frye, L.L.5    Pollard, W.T.6    Banks, J.L.7
  • 21
    • 0029912748 scopus 로고    scopus 로고
    • Development and testing of the opls all-Atom force field on conformational energetics and properties of organic liquids
    • Jorgensen, W.L.; Maxwell, D.S.; Tirado-Rives, J. Development and testing of the OPLS all-Atom force field on conformational energetics and properties of organic liquids. J. Am. Chem. Soc., 1996, 118, 1122511236.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tirado-Rives, J.3
  • 22
    • 0035913529 scopus 로고    scopus 로고
    • Evaluation and reparametrization of the opls-Aa force field for proteins via comparison with accurate quantum chemical calculations on peptides
    • Kaminski, G.A.; Friesner, R.A.; Tirado-Rives, J.; Jorgensen, W.L. Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides. J. Phys. Chem. B, 2001, 105, 64746487.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 6474-6487
    • Kaminski, G.A.1    Friesner, R.A.2    Tirado-Rives, J.3    Jorgensen, W.L.4
  • 24
    • 36449003554 scopus 로고
    • Constant pressure molecular dynamics algorithms
    • Martyna, G.J.; Tobias, D.J.; Klein, M.L. Constant pressure molecular dynamics algorithms. J. Chem. Phys., 1994, 101, 4177.
    • (1994) J. Chem. Phys. , vol.101 , pp. 4177
    • Martyna, G.J.1    Tobias, D.J.2    Klein, M.L.3
  • 25
    • 0001538909 scopus 로고
    • Canonical dynamics: Equilibrium phase-space distributions
    • Hoover, W.G. Canonical dynamics: Equilibrium phase-space distributions. Phys. Rev. A, 1985, 31, 16951697.
    • (1985) Phys. Rev. A , vol.31 , pp. 1695-1697
    • Hoover, W.G.1
  • 26
    • 0000504254 scopus 로고
    • A multiple-time-step molecular dynamics algorithm for macromolecules
    • Humphreys, D.D.; Friesner, R.A.; Berne, B.J. A multiple-time-step molecular dynamics algorithm for macromolecules. J. Phys. Chem., 1994, 98, 68856892.
    • (1994) J. Phys. Chem. , vol.98 , pp. 6885-6892
    • Humphreys, D.D.1    Friesner, R.A.2    Berne, B.J.3
  • 27
    • 0028922586 scopus 로고
    • Ligplot: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace, A.C.; Laskowski, R.A.; Thornton, J.M. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng., 1995, 8, 127134.
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 29
    • 1042287114 scopus 로고    scopus 로고
    • Skeletal muscle degeneration induced by venom phospholipases a2: Insights into the mechanisms of local and systemic myotoxicity
    • Gutierrez, J.M.; Ownby, C.L. Skeletal muscle degeneration induced by venom phospholipases A2: insights into the mechanisms of local and systemic myotoxicity. Toxicon, 2003, 42, 91531.
    • (2003) Toxicon , vol.42 , pp. 915-931
    • Gutierrez, J.M.1    Ownby, C.L.2
  • 30
    • 0024825620 scopus 로고
    • Phospholipase a2 from cobra (naja naja naja) venom. Primary structure and subspecies variation
    • Shafqat, J.; Beg, O.U.; Jornvall, H.; Zaidi, Z.H. Phospholipase A2 from cobra (Naja naja naja) venom. Primary structure and subspecies variation. Protein Seq. Data Anal., 1989, 2, 451452.
    • (1989) Protein Seq. Data Anal. , vol.2 , pp. 451-452
    • Shafqat, J.1    Beg, O.U.2    Jornvall, H.3    Zaidi, Z.H.4
  • 31
    • 0025598152 scopus 로고
    • Myotoxic components of snake venoms: Their biochemical and biological activities
    • Mebs, D.; Ownby, C.L. Myotoxic components of snake venoms: their biochemical and biological activities. Pharmacol. Ther., 1990, 48, 223236.
    • (1990) Pharmacol. Ther. , vol.48 , pp. 223-236
    • Mebs, D.1    Ownby, C.L.2
  • 32
    • 0031861230 scopus 로고    scopus 로고
    • Purification and characterization of three acidic, cytotoxic phospholipases a2 from indian cobra (naja naja naja) venom
    • Rudrammaji, L.M.; Gowda, T.V. Purification and characterization of three acidic, cytotoxic phospholipases A2 from Indian cobra (Naja naja naja) venom. Toxicon, 1998, 36, 921932.
    • (1998) Toxicon , vol.36 , pp. 921-932
    • Rudrammaji, L.M.1    Gowda, T.V.2
  • 33
    • 66349090778 scopus 로고    scopus 로고
    • Phospholipase a2 structure/function, mechanism, and signaling
    • Burke, J.E.; Dennis, E.A. Phospholipase A2 structure/function, mechanism, and signaling. J. Lipid Res., 2009, 50 Suppl, S23742.
    • (2009) J. Lipid Res. , vol.50 , Issue.SUPPL.
    • Burke, J.E.1    Dennis, E.A.2
  • 35
    • 0026074972 scopus 로고
    • Critical role of a hydrogen bond in the interaction of phospholipase a2 with transition-state and substrate analogues
    • Yu, L.; Dennis, E.A. Critical role of a hydrogen bond in the interaction of phospholipase A2 with transition-state and substrate analogues. Proc. Natl. Acad. Sci. USA, 1991, 88, 93259329.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9325-9329
    • Yu, L.1    Dennis, E.A.2
  • 36
    • 82755177579 scopus 로고    scopus 로고
    • Inhibitory effects of plant phenolic compounds on enzymatic and cytotoxic activities induced by a snake venom phospholipase a2
    • Pereanez, J.A.; Nunez, V.; Patino, A.C.; Londono, M.; Quintana, J.C. Inhibitory effects of plant phenolic compounds on enzymatic and cytotoxic activities induced by a snake venom phospholipase A2. Vitae, 2011, 18, 295304.
    • (2011) Vitae , vol.18 , pp. 295-304
    • Pereanez, J.A.1    Nunez, V.2    Patino, A.C.3    Londono, M.4    Quintana, J.C.5
  • 37
    • 0024347150 scopus 로고
    • Studies on the status of lysine residues in phospholipase a2 from naja naja atra (taiwan cobra) snake venom
    • Yang, C.C.; Chang, L.S. Studies on the status of lysine residues in phospholipase A2 from Naja naja atra (Taiwan cobra) snake venom. Biochem J., 1989, 262, 855860.
    • (1989) Biochem J. , vol.262 , pp. 855-860
    • Yang, C.C.1    Chang, L.S.2
  • 38
    • 0024452930 scopus 로고
    • Degradation of extracellular matrix proteins by hemorrhagic metalloproteinases
    • Baramova, E.N.; Shannon, J.D; Bjarnason J.B.; Fox J.W. Degradation of extracellular matrix proteins by hemorrhagic metalloproteinases. Arch. Biochem. Biophys., 1989, 275, 6371.
    • (1989) Arch. Biochem. Biophys. , vol.275 , pp. 63-71
    • Baramova, E.N.1    Shannon, J.D.2    Bjarnason, J.B.3    Fox, J.W.4
  • 39
    • 0017883906 scopus 로고
    • Hemorrhagic toxins from western diamondback rattlesnake (crotalus atrox) venom: Isolation and characterization of five toxins and the role of zinc in hemorrhagic toxin e
    • Bjarnason, J.B.; Tu, A.T. Hemorrhagic toxins from Western diamondback rattlesnake (Crotalus atrox) venom: isolation and characterization of five toxins and the role of zinc in hemorrhagic toxin e. Biochemistry, 1978, 17, 33953404.
    • (1978) Biochemistry , vol.17 , pp. 3395-3404
    • Bjarnason, J.B.1    Tu, A.T.2
  • 40
    • 0028146808 scopus 로고
    • Hemorrhagic metalloproteinases from snake venoms
    • Bjarnason, J.B.; Fox, J.W. Hemorrhagic metalloproteinases from snake venoms. Pharmacol. Therapeut., 1994, 62, 325372.
    • (1994) Pharmacol. Therapeut. , vol.62 , pp. 325-372
    • Bjarnason, J.B.1    Fox, J.W.2
  • 42
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter, I.; Berger, A. On the size of the active site in proteases. I. Papain. Biochem Biophys Res Commun., 1967, 27, 157162.
    • (1967) Biochem Biophys Res Commun. , Issue.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 43
    • 0029866390 scopus 로고    scopus 로고
    • Batimastat a potent matrix mealloproteinase inhibitor, exhibits an unexpected mode of binding
    • Botos, I.; Scapozza, L.; Zhang, D.; Liotta, L.A.; Meyer, E.F. Batimastat, a potent matrix mealloproteinase inhibitor, exhibits an unexpected mode of binding. Proc Natl Acad Sci USA, 1996, 93, 27492754.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 2749-2754
    • Botos, I.1    Scapozza, L.2    Zhang, D.3    Liotta, L.A.4    Meyer, E.F.5
  • 45
    • 33846906016 scopus 로고    scopus 로고
    • Matrix metalloproteinases (mmps): Chemical-biological functions and (q)sars
    • Verma, R.P.; Hansch, C. Matrix metalloproteinases (MMPs): chemical-biological functions and (Q)SARs. Bioorg Med Chem., 2007, 15, 22232268.
    • (2007) Bioorg Med Chem. , vol.15 , pp. 2223-2268
    • Verma, R.P.1    Hansch, C.2
  • 46
    • 0001651169 scopus 로고    scopus 로고
    • Design and therapeutic application of matrix metalloproteinase inhibitors
    • Whittaker, M.; Floyd, C.D.; Brown, P.; Gearing, A.J. Design and therapeutic application of matrix metalloproteinase inhibitors. Chem Rev., 1999, 99, 27352776.
    • (1999) Chem Rev. , vol.99 , pp. 2735-2776
    • Whittaker, M.1    Floyd, C.D.2    Brown, P.3    Gearing, A.J.4
  • 47
    • 0346364657 scopus 로고    scopus 로고
    • Amino acid properties and consequences of substitutions
    • Betts, M.J.; Russell, R.B. Amino Acid Properties and Consequences of Substitutions. Bioinform. Genet., 2003, 317, 289.
    • (2003) Bioinform. Genet. , vol.317 , pp. 289
    • Betts, M.J.1    Russell, R.B.2


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