메뉴 건너뛰기




Volumn 53, Issue 1, 2010, Pages 106-118

Antiangiogenic effect of dual/selective α5 β1/αvβ3 integrin antagonists designed on partially modified retro-inverso cyclotetrapeptide mimetics

Author keywords

[No Author keywords available]

Indexed keywords

ANGIOGENESIS INHIBITOR; CYCLOPEPTIDE; FIBRONECTIN; TETRAPEPTIDE; VERY LATE ACTIVATION ANTIGEN 5; VITRONECTIN; VITRONECTIN RECEPTOR;

EID: 74849140343     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm9013532     Document Type: Article
Times cited : (29)

References (80)
  • 1
    • 0032829104 scopus 로고    scopus 로고
    • Tumor angiogenesis, new drugs on the block
    • Brower, V. Tumor angiogenesis, new drugs on the block. Nat. Biotechnol. 1999, 17, 963-968.
    • (1999) Nat. Biotechnol , vol.17 , pp. 963-968
    • Brower, V.1
  • 2
    • 74849112306 scopus 로고    scopus 로고
    • Arndt, T.; Arndt, U.; Reuning, U.; Kessler, H. Integrins in angiogenesis: Implications for tumor therapy. In Cancer Therapy: Molecular Targets in Tumor-Host Interactions; Weber, G. F., Ed.; Horizon Bioscience: Norfolk, U.K., 2005.
    • Arndt, T.; Arndt, U.; Reuning, U.; Kessler, H. Integrins in angiogenesis: Implications for tumor therapy. In Cancer Therapy: Molecular Targets in Tumor-Host Interactions; Weber, G. F., Ed.; Horizon Bioscience: Norfolk, U.K., 2005.
  • 4
    • 0028362876 scopus 로고
    • Requirement of vascular integrin αvβ3 for angiogenesis
    • Brooks, P. C.; Clark, R. A.; Cheresh, D. A. Requirement of vascular integrin αvβ3 for angiogenesis. Science 1994, 264, 569-571.
    • (1994) Science , vol.264 , pp. 569-571
    • Brooks, P.C.1    Clark, R.A.2    Cheresh, D.A.3
  • 5
    • 0036734093 scopus 로고    scopus 로고
    • Areevaluation of integrins as regulators of angiogenesis
    • Hynes, R. O. Areevaluation of integrins as regulators of angiogenesis. Nat. Med. 2002, 8, 918-921.
    • (2002) Nat. Med , vol.8 , pp. 918-921
    • Hynes, R.O.1
  • 7
    • 0009209980 scopus 로고    scopus 로고
    • Peptide inhibitors of β1 integrins
    • Peltz, G, Ed, Springer: Heidelberg, Germany
    • Cardarelli, P. M.; Lobl, T. J. Peptide inhibitors of β1 integrins. In Leukocyte Recruitment in Inflammatory Diseases; Peltz, G., Ed.; Springer: Heidelberg, Germany, 1996; pp 275-294.
    • (1996) Leukocyte Recruitment in Inflammatory Diseases , pp. 275-294
    • Cardarelli, P.M.1    Lobl, T.J.2
  • 8
    • 0029876080 scopus 로고    scopus 로고
    • Integrin signaling and matrix assembly
    • Ruoslahti, E. Integrin signaling and matrix assembly. Tumor Biol. 1996, 17, 117-124.
    • (1996) Tumor Biol , vol.17 , pp. 117-124
    • Ruoslahti, E.1
  • 9
    • 0030870211 scopus 로고    scopus 로고
    • A matrix form of fibronectin mediates enhanced binding of Streptococcus pyogenes to host tissue
    • Okada, N.; Watarai, M.; Ozeri, V.; Hanski, E.; Caparon, M.; Sasakawa, C. A matrix form of fibronectin mediates enhanced binding of Streptococcus pyogenes to host tissue. J. Biol. Chem. 1997, 272, 26978-26984.
    • (1997) J. Biol. Chem , vol.272 , pp. 26978-26984
    • Okada, N.1    Watarai, M.2    Ozeri, V.3    Hanski, E.4    Caparon, M.5    Sasakawa, C.6
  • 10
    • 0034721888 scopus 로고    scopus 로고
    • Regulation of integrin αvβ3-mediated endothelial cell migration and angiogenesis by integrin α5β1 and protein kinase A
    • Kim, S.; Harris, M.; Varner, J. A. Regulation of integrin αvβ3-mediated endothelial cell migration and angiogenesis by integrin α5β1 and protein kinase A. J. Biol. Chem. 2000, 275, 33920-33928.
    • (2000) J. Biol. Chem , vol.275 , pp. 33920-33928
    • Kim, S.1    Harris, M.2    Varner, J.A.3
  • 11
    • 0033626573 scopus 로고    scopus 로고
    • Role of α5β1 and αvβ3 integrins on smooth muscle cell spreading and migration in fibrin gels
    • Ikari, Y.; Yee, K. O.; Schwartz, S. M. Role of α5β1 and αvβ3 integrins on smooth muscle cell spreading and migration in fibrin gels. Thromb. Haemostasis 2000, 84, 701-705.
    • (2000) Thromb. Haemostasis , vol.84 , pp. 701-705
    • Ikari, Y.1    Yee, K.O.2    Schwartz, S.M.3
  • 12
    • 33746891461 scopus 로고    scopus 로고
    • Adhesion dependent signalling in the tumour microenvironment: The future of drug targeting
    • Bewick, M. A.; Lafrenie, R. M. Adhesion dependent signalling in the tumour microenvironment: The future of drug targeting. Curr. Pharm. Des. 2006, 12, 2833-2848.
    • (2006) Curr. Pharm. Des , vol.12 , pp. 2833-2848
    • Bewick, M.A.1    Lafrenie, R.M.2
  • 13
    • 0033866240 scopus 로고    scopus 로고
    • Use of gastrin-releasing peptide promoter for specific expression of thymidine kinase gene in small-cell lung carcinoma cell
    • Mitjans, F.; Meyer, T.; Fittschen, C.; Goodman, S.; Jonczyk, A.; Marshall, J. F.; Reyes, G.; Piulats, J. Use of gastrin-releasing peptide promoter for specific expression of thymidine kinase gene in small-cell lung carcinoma cell. Int. J. Cancer 2000, 87, 716-723.
    • (2000) Int. J. Cancer , vol.87 , pp. 716-723
    • Mitjans, F.1    Meyer, T.2    Fittschen, C.3    Goodman, S.4    Jonczyk, A.5    Marshall, J.F.6    Reyes, G.7    Piulats, J.8
  • 15
    • 0029775681 scopus 로고    scopus 로고
    • Ruoslahti, E. RGD and other recognition sequences for integrins. Annu. Rev. Cell Dev. Biol. 1996, 12, 697-715.
    • Ruoslahti, E. RGD and other recognition sequences for integrins. Annu. Rev. Cell Dev. Biol. 1996, 12, 697-715.
  • 16
    • 36949010979 scopus 로고    scopus 로고
    • Identification of novel drug targets for angiostatic cancer therapy; it takes two to tango
    • Thijssen, V. L. J. L.; van Beijnum, J. R.; Mayo, K. H.; Griffioen, A. W. Identification of novel drug targets for angiostatic cancer therapy; it takes two to tango. Curr. Pharm. Des. 2007, 13, 3576-3583.
    • (2007) Curr. Pharm. Des , vol.13 , pp. 3576-3583
    • Thijssen, V.L.J.L.1    van Beijnum, J.R.2    Mayo, K.H.3    Griffioen, A.W.4
  • 17
    • 44349130354 scopus 로고    scopus 로고
    • Anti-adhesion evolves to a promising therapeutic concept in oncology
    • Schmidmaier, R.; Baumann, P. Anti-adhesion evolves to a promising therapeutic concept in oncology. Curr. Med. Chem. 2008, 15, 978-990.
    • (2008) Curr. Med. Chem , vol.15 , pp. 978-990
    • Schmidmaier, R.1    Baumann, P.2
  • 18
    • 0023058313 scopus 로고    scopus 로고
    • Ruoslahti, E.; Pierschbacher, M. D. Arg-Gly-Asp: A versatile cell recognition signal. Cell 1986, 44, 517-518.
    • Ruoslahti, E.; Pierschbacher, M. D. Arg-Gly-Asp: A versatile cell recognition signal. Cell 1986, 44, 517-518.
  • 19
    • 0025814801 scopus 로고
    • Arginyl-glycylaspartic acid (RGD): A cell-adhesion motif
    • DeSouza, S. E.; Ginsberg, M. H.; Plow, E. F. Arginyl-glycylaspartic acid (RGD): A cell-adhesion motif. Trends Biochem. Sci. 1991, 16, 246-250.
    • (1991) Trends Biochem. Sci , vol.16 , pp. 246-250
    • DeSouza, S.E.1    Ginsberg, M.H.2    Plow, E.F.3
  • 20
    • 0041997867 scopus 로고    scopus 로고
    • 3 integrin antagonists: Chemical and structural requirements for activity and selectivity
    • 3 integrin antagonists: Chemical and structural requirements for activity and selectivity. Mini-Rev. Med. Chem. 2002, 2, 531-42.
    • (2002) Mini-Rev. Med. Chem , vol.2 , pp. 531-542
    • Henry, C.1    Moitessier, N.2    Chapleur, Y.3
  • 22
    • 11844302202 scopus 로고    scopus 로고
    • Non peptidic αvβ3 antagonists: Recent developments
    • Cacciari, B.; Spallato, G. Non peptidic αvβ3 antagonists: Recent developments. Curr. Med. Chem. 2005, 12, 51-70.
    • (2005) Curr. Med. Chem , vol.12 , pp. 51-70
    • Cacciari, B.1    Spallato, G.2
  • 23
    • 0027997413 scopus 로고
    • Selective recognition of cyclic RGD peptides of NMR defined conformation by αIIbβ3, αVβ3, and α5β1 integrins
    • Pfaff, M.; Tangemann, K.; Müller, B.; Gurrath, M.; Müller, G.; Kessler, H.; Timpl, R.; Engel, J. Selective recognition of cyclic RGD peptides of NMR defined conformation by αIIbβ3, αVβ3, and α5β1 integrins. J. Biol. Chem. 1994, 269, 20233-20238.
    • (1994) J. Biol. Chem , vol.269 , pp. 20233-20238
    • Pfaff, M.1    Tangemann, K.2    Müller, B.3    Gurrath, M.4    Müller, G.5    Kessler, H.6    Timpl, R.7    Engel, J.8
  • 24
    • 0027102818 scopus 로고
    • Conformation/activity studies of rationally designed anti-adhesive RGD peptides
    • Gurrath, M.; Müller, G.; Kessler, H.; Aumailley, M.; Timpl, R. Conformation/activity studies of rationally designed anti-adhesive RGD peptides. Eur. J. Biochem. 1992, 210, 911-921.
    • (1992) Eur. J. Biochem , vol.210 , pp. 911-921
    • Gurrath, M.1    Müller, G.2    Kessler, H.3    Aumailley, M.4    Timpl, R.5
  • 27
    • 33748616254 scopus 로고    scopus 로고
    • Cai, W.; Chen, X. Anti-angiogenic cancer therapy based on integrin αvβ3 antagonism. Anticancer Agents Med. Chem. 2006, 6, 407-428.
    • Cai, W.; Chen, X. Anti-angiogenic cancer therapy based on integrin αvβ3 antagonism. Anticancer Agents Med. Chem. 2006, 6, 407-428.
  • 28
    • 35148840122 scopus 로고    scopus 로고
    • Design and chemical synthesis of integrin ligands
    • Heckmann, D.; Kessler, H. Design and chemical synthesis of integrin ligands. Methods Enzymol. 2007, 426, 463-503.
    • (2007) Methods Enzymol , vol.426 , pp. 463-503
    • Heckmann, D.1    Kessler, H.2
  • 29
    • 0037023363 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin αvβ3 in complex with an Arg-Gly-Asp ligand
    • Xiong, J.-P.; Stehle, T.; Zhang, R.; Joachimiak, A.; Frech, M.; Goodman, S. L.; Amin Arnaout, M. Crystal structure of the extracellular segment of integrin αvβ3 in complex with an Arg-Gly-Asp ligand. Science 2002, 296, 151-155.
    • (2002) Science , vol.296 , pp. 151-155
    • Xiong, J.-P.1    Stehle, T.2    Zhang, R.3    Joachimiak, A.4    Frech, M.5    Goodman, S.L.6    Amin Arnaout, M.7
  • 30
    • 0141958105 scopus 로고    scopus 로고
    • Docking studies on αvβ3 integrin ligands: Pharmacophore refinement and implications for drug design
    • Marinelli, L.; Lavecchia, A.; Gottschalk, K.-E.; Novellino, E.; Kessler, H. Docking studies on αvβ3 integrin ligands: Pharmacophore refinement and implications for drug design. J. Med. Chem. 2003, 46, 4393-4404.
    • (2003) J. Med. Chem , vol.46 , pp. 4393-4404
    • Marinelli, L.1    Lavecchia, A.2    Gottschalk, K.-E.3    Novellino, E.4    Kessler, H.5
  • 34
    • 0141625303 scopus 로고    scopus 로고
    • Structure of integrin α5β1 in complex with fibronectin
    • Takagi, J.; Strokovich, K.; Springer, T. A.; Walz, T. Structure of integrin α5β1 in complex with fibronectin. EMBO J. 2003, 22, 4607-4615.
    • (2003) EMBO J , vol.22 , pp. 4607-4615
    • Takagi, J.1    Strokovich, K.2    Springer, T.A.3    Walz, T.4
  • 37
    • 21244467582 scopus 로고    scopus 로고
    • Ligand binding analysis for human α5β1 integrin: Strategies for designing new a5b1 integrin antagonists
    • Marinelli, L.; Meyer, A.; Heckmann, D.; Lavecchia, A.; Novellino, E.; Kessler, H. Ligand binding analysis for human α5β1 integrin: Strategies for designing new a5b1 integrin antagonists. J. Med. Chem. 2005, 48, 4204-4207.
    • (2005) J. Med. Chem , vol.48 , pp. 4204-4207
    • Marinelli, L.1    Meyer, A.2    Heckmann, D.3    Lavecchia, A.4    Novellino, E.5    Kessler, H.6
  • 38
    • 34250792823 scopus 로고    scopus 로고
    • Probing integrin selectivity: Rational design of highly active and selective ligands for the α5β1 and αvβ3 integrin receptor
    • Heckmann, D.; Meyer, A.; Marinelli, L.; Zahn, G.; Stragies, R.; Kessler, H. Probing integrin selectivity: Rational design of highly active and selective ligands for the α5β1 and αvβ3 integrin receptor. Angew. Chem., Int. Ed. 2007, 46, 3571-3574.
    • (2007) Angew. Chem., Int. Ed , vol.46 , pp. 3571-3574
    • Heckmann, D.1    Meyer, A.2    Marinelli, L.3    Zahn, G.4    Stragies, R.5    Kessler, H.6
  • 41
    • 0034614056 scopus 로고    scopus 로고
    • Are β-amino acids γ-turn mimetics? Exploring a new design principle for bioactive cyclopeptides
    • Schumann, F.; Muller, A.; Koksch, M.; Muller, G.; Sewald, N. Are β-amino acids γ-turn mimetics? Exploring a new design principle for bioactive cyclopeptides. J. Am. Chem. Soc. 2000, 122, 12009-12010.
    • (2000) J. Am. Chem. Soc , vol.122 , pp. 12009-12010
    • Schumann, F.1    Muller, A.2    Koksch, M.3    Muller, G.4    Sewald, N.5
  • 42
    • 0000845126 scopus 로고
    • A dozen years of retro-inverso peptidomimetics
    • Chorev, M.; Goodman, M. A dozen years of retro-inverso peptidomimetics. Acc. Chem. Res. 1993, 26, 266-273.
    • (1993) Acc. Chem. Res , vol.26 , pp. 266-273
    • Chorev, M.1    Goodman, M.2
  • 43
    • 20344370972 scopus 로고    scopus 로고
    • The partial retro-inverso modification: A road traveled together
    • Chorev, M. The partial retro-inverso modification: A road traveled together. Biopolymers 2005, 80, 67-84.
    • (2005) Biopolymers , vol.80 , pp. 67-84
    • Chorev, M.1
  • 44
    • 0037178340 scopus 로고    scopus 로고
    • Ni-to -Ni+3-ethylene-bridged partially modified retro-inverso tetrapeptide β-turn mimetic: Design, synthesis, and structural characterization
    • Han, Y.; Giragossian, C.; Mierke, D. F.; Chorev, M. Ni-to -Ni+3-ethylene-bridged partially modified retro-inverso tetrapeptide β-turn mimetic: Design, synthesis, and structural characterization. J. Org. Chem. 2002, 67, 5085-5097.
    • (2002) J. Org. Chem , vol.67 , pp. 5085-5097
    • Han, Y.1    Giragossian, C.2    Mierke, D.F.3    Chorev, M.4
  • 45
    • 33846227460 scopus 로고    scopus 로고
    • Lee, Y. S.; Agnes, R. S.; Davis, P.; Ma, S.-w.; Badghisi, H.; Lai, J.; Porreca, F.; Hruby, V, J. Partial retro-inverso, retro, and inverso modifications of hydrazide linked bifunctional peptides for opioid and cholecystokinin (CCK) receptors. J. Med. Chem. 2007, 50, 165-168.
    • Lee, Y. S.; Agnes, R. S.; Davis, P.; Ma, S.-w.; Badghisi, H.; Lai, J.; Porreca, F.; Hruby, V, J. Partial retro-inverso, retro, and inverso modifications of hydrazide linked bifunctional peptides for opioid and cholecystokinin (CCK) receptors. J. Med. Chem. 2007, 50, 165-168.
  • 46
    • 0011822184 scopus 로고    scopus 로고
    • Partially modified retro-inverso peptides: Development, synthesis, and conformational behavior
    • Fletcher, M. D.; Campbell, M. M. Partially modified retro-inverso peptides: Development, synthesis, and conformational behavior. Chem. Rev. 1998, 98, 763-795.
    • (1998) Chem. Rev , vol.98 , pp. 763-795
    • Fletcher, M.D.1    Campbell, M.M.2
  • 47
    • 0037460144 scopus 로고    scopus 로고
    • Conformationally homogeneous cyclic tetrapeptides: Useful new three-dimensional scaffolds
    • Glenn, M. P.; Kelso, M. J.; Tyndall, J. D. A.; Fairlie, D. P. Conformationally homogeneous cyclic tetrapeptides: Useful new three-dimensional scaffolds. J. Am. Chem. Soc. 2003, 125, 640-641.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 640-641
    • Glenn, M.P.1    Kelso, M.J.2    Tyndall, J.D.A.3    Fairlie, D.P.4
  • 48
    • 33750430831 scopus 로고    scopus 로고
    • β2-Amino acids in the design of conformationally homogeneous cyclo-peptide scaffolds
    • Norgren, A. S.; Buttner, F.; Prabpai, S.; Kongsaeree, P.; Arvidsson, P. I. β2-Amino acids in the design of conformationally homogeneous cyclo-peptide scaffolds. J. Org. Chem. 2006, 71, 6814-6821.
    • (2006) J. Org. Chem , vol.71 , pp. 6814-6821
    • Norgren, A.S.1    Buttner, F.2    Prabpai, S.3    Kongsaeree, P.4    Arvidsson, P.I.5
  • 51
    • 0024287092 scopus 로고
    • The preparation of a partially protected heptasaccharide-asparagine intermediate for glycopeptide synthesis
    • Nakabayashi, S.; Warren, C. D.; Jeanloz, R. W. The preparation of a partially protected heptasaccharide-asparagine intermediate for glycopeptide synthesis. Carbohydr. Res. 1988, 174, 279-289.
    • (1988) Carbohydr. Res , vol.174 , pp. 279-289
    • Nakabayashi, S.1    Warren, C.D.2    Jeanloz, R.W.3
  • 53
    • 0141483383 scopus 로고    scopus 로고
    • Adhesion-dependent activation of the ERK1/2 cascade is by-passed in melanoma cells
    • Conner, S. R.; Scott, G.; Aplin, A. E. Adhesion-dependent activation of the ERK1/2 cascade is by-passed in melanoma cells. J. Biol. Chem. 2003, 278, 34548-34554.
    • (2003) J. Biol. Chem , vol.278 , pp. 34548-34554
    • Conner, S.R.1    Scott, G.2    Aplin, A.E.3
  • 54
    • 57149126267 scopus 로고    scopus 로고
    • Tumor endothelial cell targeted cyclic RGDmodified heparin derivative: Inhibition of angiogenesis and tumor growth
    • Park, K.; Kim, Y.-S.; Lee, G. Y.; Parl, R.-W.; Kim, I.-S.; Kim, S. Y.; Byun, Y. Tumor endothelial cell targeted cyclic RGDmodified heparin derivative: Inhibition of angiogenesis and tumor growth. Pharm. Res. 2008, 25, 2786-2798.
    • (2008) Pharm. Res , vol.25 , pp. 2786-2798
    • Park, K.1    Kim, Y.-S.2    Lee, G.Y.3    Parl, R.-W.4    Kim, I.-S.5    Kim, S.Y.6    Byun, Y.7
  • 55
    • 0029665151 scopus 로고    scopus 로고
    • Activation-dependent α5β1 integrin-mediated adhesion to fibronectin decreases proliferation of chronic myelogenous leukemia progenitors and K562 cells
    • Lundell, B. I.; McCarthy, J. B.; Kovach, N. L.; Verfaillie, C. M. Activation-dependent α5β1 integrin-mediated adhesion to fibronectin decreases proliferation of chronic myelogenous leukemia progenitors and K562 cells. Blood 1996, 87, 2450-2458.
    • (1996) Blood , vol.87 , pp. 2450-2458
    • Lundell, B.I.1    McCarthy, J.B.2    Kovach, N.L.3    Verfaillie, C.M.4
  • 58
    • 0030893498 scopus 로고    scopus 로고
    • Integrin antagonists and other low molecular weight compounds as inhibitors of angiogenesis: New drugs in cancer therapy
    • Giannis, A.; Rubsam, F. Integrin antagonists and other low molecular weight compounds as inhibitors of angiogenesis: New drugs in cancer therapy. Angew. Chem., Int. Ed. 1997, 36, 588-590.
    • (1997) Angew. Chem., Int. Ed , vol.36 , pp. 588-590
    • Giannis, A.1    Rubsam, F.2
  • 60
    • 0005306564 scopus 로고
    • Human endothelial cells synthesize and express an Arg-Gly-Asp-directed adhesion receptor involved in attachment to fibrinogen and von Willebrand factor
    • Cheresh, D. A. Human endothelial cells synthesize and express an Arg-Gly-Asp-directed adhesion receptor involved in attachment to fibrinogen and von Willebrand factor. Proc. Natl. Acad. Sci. U.S. A. 1987, 84, 6471-6475.
    • (1987) Proc. Natl. Acad. Sci. U.S. A , vol.84 , pp. 6471-6475
    • Cheresh, D.A.1
  • 62
    • 0033886323 scopus 로고    scopus 로고
    • Angiogenesis in cancer and other diseases
    • Carmelit, P.; Jain, R. K. Angiogenesis in cancer and other diseases. Circ. Res. 2000, 87, 176-178.
    • (2000) Circ. Res , vol.87 , pp. 176-178
    • Carmelit, P.1    Jain, R.K.2
  • 63
    • 0026027556 scopus 로고
    • Cancer metastasis and angiogenesis: An imbalance of positive and negative regulation
    • Liotta, L.; Steeg, P.; Stetler-Stevenson, W. Cancer metastasis and angiogenesis: An imbalance of positive and negative regulation. Cell 1991, 64, 327-336.
    • (1991) Cell , vol.64 , pp. 327-336
    • Liotta, L.1    Steeg, P.2    Stetler-Stevenson, W.3
  • 64
    • 0030576517 scopus 로고    scopus 로고
    • Patterns and emerging mechanisms of the angiogenic switch during tumorigenesis
    • Hanahan, D.; Folkman, J. Patterns and emerging mechanisms of the angiogenic switch during tumorigenesis. Cell 1996, 86, 353-364.
    • (1996) Cell , vol.86 , pp. 353-364
    • Hanahan, D.1    Folkman, J.2
  • 65
    • 0020163940 scopus 로고
    • Conformation and biological activity of cyclic peptide
    • Kessler, H. Conformation and biological activity of cyclic peptide. Angew. Chem., Int. Ed. 1982, 21, 512-523.
    • (1982) Angew. Chem., Int. Ed , vol.21 , pp. 512-523
    • Kessler, H.1
  • 66
    • 0025156939 scopus 로고
    • Cyclic pentapeptides as models for reverse turns: Determination of the equilibrium distribution between type I and type II conformations of Pro-Asn and Pro-Ala β-turns
    • Stradley, S. J.; Rizo, J.; Bruch, M. D.; Stroup, A. N.; Gierasch, L. M. Cyclic pentapeptides as models for reverse turns: Determination of the equilibrium distribution between type I and type II conformations of Pro-Asn and Pro-Ala β-turns. Biopolymers 1990, 29, 263-287.
    • (1990) Biopolymers , vol.29 , pp. 263-287
    • Stradley, S.J.1    Rizo, J.2    Bruch, M.D.3    Stroup, A.N.4    Gierasch, L.M.5
  • 67
    • 0026848961 scopus 로고    scopus 로고
    • 2O mixture as a biomimetic medium, see: Temussi, P. A.; Picone, D.; Saviano, G.; Amodeo, P.; Motta, A.; Tancredi, T.; Salvadori, S.; Tomatis, R. Conformational analysis of an opioid peptide in solvent media that mimic cytoplasm viscosity. Biopolymers 1992, 32, 367-372 and references cited herein .
    • 2O mixture as a biomimetic medium, see: Temussi, P. A.; Picone, D.; Saviano, G.; Amodeo, P.; Motta, A.; Tancredi, T.; Salvadori, S.; Tomatis, R. Conformational analysis of an opioid peptide in solvent media that mimic cytoplasm viscosity. Biopolymers 1992, 32, 367-372 and references cited herein .
  • 68
    • 0019267144 scopus 로고
    • Intramolecularly hydrogen-bonded peptide conformations
    • Toniolo, C. Intramolecularly hydrogen-bonded peptide conformations. CRC Crit. Rev. Biochem. 1980, 9, 1-44.
    • (1980) CRC Crit. Rev. Biochem , vol.9 , pp. 1-44
    • Toniolo, C.1
  • 69
    • 74849129774 scopus 로고    scopus 로고
    • HyperChem, release 8.0.3; Hypercube Inc, Gainesville, FL, 2007
    • HyperChem, release 8.0.3; Hypercube Inc.: Gainesville, FL, 2007.
  • 70
    • 0029011701 scopus 로고    scopus 로고
    • Cornell, W. D.; Cieplak, P.; Bayly, C. I.; Gould, I. R.; Merz, K. M.; Ferguson, D. M.; Spellmeyer, D. C.; Fox, T.; Caldwell, J. W.; Kollman, P. A. A second generation force field for the simulation of proteins, nucleic acids, and organic molecules. J. Am. Chem. Soc. 1995, 117, 5179-5197.
    • Cornell, W. D.; Cieplak, P.; Bayly, C. I.; Gould, I. R.; Merz, K. M.; Ferguson, D. M.; Spellmeyer, D. C.; Fox, T.; Caldwell, J. W.; Kollman, P. A. A second generation force field for the simulation of proteins, nucleic acids, and organic molecules. J. Am. Chem. Soc. 1995, 117, 5179-5197.
  • 71
    • 74849103190 scopus 로고    scopus 로고
    • In a preliminary investigation of the conformational features of the PMRI RGD mimetics by ROESY and MD, we analyzed the insolution structural features of c[βPheψ(NHCO)Asp(Ot-Bu)ψ-(NHCO)Gly-Arg(Mtr, 14) and c[(R)-βPheψ(NHCO)Asp(Ot-Bu)ψ(NHCO)Gly-Arg(Mtr, the protected synthetic precursors of 2 and 3, respectively. While the conformation of fully protected 2 (14) was practically coincident to the type I β-turn/ type I β-turn structure of 2 (Figures 5 and 6, the predominant conformation of fully protected 3 was compatible with the inverse γ/inverse γ structure reported in Figure 8. Apparently, increasing the size of the side chains of the PMRI CTPs tends to stabilize the inverse γ/ inverse γ structure over the type II β-turn structure Figure 8
    • In a preliminary investigation of the conformational features of the PMRI RGD mimetics by ROESY and MD, we analyzed the insolution structural features of c[βPheψ(NHCO)Asp(Ot-Bu)ψ-(NHCO)Gly-Arg(Mtr)] (14) and c[(R)-βPheψ(NHCO)Asp(Ot-Bu)ψ(NHCO)Gly-Arg(Mtr)], the protected synthetic precursors of 2 and 3, respectively. While the conformation of fully protected 2 (14) was practically coincident to the type I β-turn/ type I β-turn structure of 2 (Figures 5 and 6), the predominant conformation of fully protected 3 was compatible with the inverse γ/inverse γ structure reported in Figure 8. Apparently, increasing the size of the side chains of the PMRI CTPs tends to stabilize the inverse γ/ inverse γ structure over the type II β-turn structure (Figure 8).
  • 72
    • 74849122511 scopus 로고    scopus 로고
    • Glide, version 4.5; Schrödinger, LLC: New York, 2007
    • Glide, version 4.5; Schrödinger, LLC: New York, 2007.
  • 73
    • 0028670833 scopus 로고
    • 3 antagonists promote tumour regression by inducing apoptosis of angiogenic blood vessels
    • 3 antagonists promote tumour regression by inducing apoptosis of angiogenic blood vessels. Cell 1994, 79, 1157-1164.
    • (1994) Cell , vol.79 , pp. 1157-1164
    • Brooks, P.C.1    Montgomery, A.M.P.2    Rosenfeld, M.3
  • 74
    • 0033843942 scopus 로고    scopus 로고
    • Regulation of angiogenesis in vivo by ligation of integrin α5β1 with the central cell-binding domain of fibronectin
    • Kim, S.; Bell, K.; Mousa, S.; Varner, J. A. Regulation of angiogenesis in vivo by ligation of integrin α5β1 with the central cell-binding domain of fibronectin. Am. J. Pathol. 2000, 156, 1345-1362.
    • (2000) Am. J. Pathol , vol.156 , pp. 1345-1362
    • Kim, S.1    Bell, K.2    Mousa, S.3    Varner, J.A.4
  • 75
    • 0028790294 scopus 로고
    • Phorbol ester (TPA)-induced differential modulation of cell surface antigens in human pluripotential leukemia (K-562) cell line: Effects of protein kinase inhibitors with broad and PKC selective inhibitory activity
    • Hunakova, L.; Sedlak, J.; Klobusicka, M.; Sulikova, M.; Chorvath, B. Phorbol ester (TPA)-induced differential modulation of cell surface antigens in human pluripotential leukemia (K-562) cell line: Effects of protein kinase inhibitors with broad and PKC selective inhibitory activity. Neoplasma 1995, 42, 249-253.
    • (1995) Neoplasma , vol.42 , pp. 249-253
    • Hunakova, L.1    Sedlak, J.2    Klobusicka, M.3    Sulikova, M.4    Chorvath, B.5
  • 77
    • 0030586236 scopus 로고    scopus 로고
    • Rate assay of N-acetyl-β-D- hexosaminidase with 4-nitrophenyl N-acetyl-β-D-glucosaminide as an artificial substrate
    • Shibata, H.; Yagi, T. Rate assay of N-acetyl-β-D- hexosaminidase with 4-nitrophenyl N-acetyl-β-D-glucosaminide as an artificial substrate. Clin. Chim. Acta 1996, 251, 53-64.
    • (1996) Clin. Chim. Acta , vol.251 , pp. 53-64
    • Shibata, H.1    Yagi, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.