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Volumn 39, Issue 10, 1996, Pages 2008-2017

Rational design of true hirudin mimetics: Synthesis and characterization of multisite-directed α-thrombin inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

HIRUDIN DERIVATIVE; HIRUNORM IV; HIRUNORM V; THROMBIN INHIBITOR; UNCLASSIFIED DRUG;

EID: 0029984910     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm950898g     Document Type: Article
Times cited : (27)

References (64)
  • 1
    • 15844380418 scopus 로고    scopus 로고
    • note
    • R, retention time; aPTT, activated partial thromboplastin time; PT, prothrombin time; TT, thromboplastin time; BSA, bovine serum albumine; ATU, antithrombin units.
  • 3
    • 0026102830 scopus 로고
    • Thrombin structure and function: Why thrombin is the primary target for antithrombotics
    • (b) Fenton, J. W., II; Ofosu, F. A.; Moon, D. G.; Maraganore, J. M. Thrombin structure and function: Why thrombin is the primary target for antithrombotics. Blood Coag. Fibrinol. 1991, 2, 69-75.
    • (1991) Blood Coag. Fibrinol. , vol.2 , pp. 69-75
    • Fenton II, J.W.1    Ofosu, F.A.2    Moon, D.G.3    Maraganore, J.M.4
  • 6
    • 0000319455 scopus 로고
    • Hirudin is an inhibitor of thrombin
    • (a) Markwardt, F. Hirudin is an inhibitor of thrombin. Methods Enzymol. 1970, 19, 924-932.
    • (1970) Methods Enzymol. , vol.19 , pp. 924-932
    • Markwardt, F.1
  • 7
    • 0019801424 scopus 로고
    • Biochemische und pharmakologische aspekte des thrombininhibitors hirudin
    • (b) Walsmann, P.; Markwardt, F. Biochemische und pharmakologische aspekte des thrombininhibitors hirudin. Pharmazie 1981, 36, 653-660.
    • (1981) Pharmazie , vol.36 , pp. 653-660
    • Walsmann, P.1    Markwardt, F.2
  • 8
    • 0027968823 scopus 로고
    • The development of hirudin as an antithrombotic drug
    • (c) Markwardt, F. The development of hirudin as an antithrombotic drug. Thrombosis Res. 1994, 74, 1-23.
    • (1994) Thrombosis Res. , vol.74 , pp. 1-23
    • Markwardt, F.1
  • 10
    • 0025174706 scopus 로고
    • Inhibition of coagulation and thrombin induced platelet activities by a synthetic dodecapeptide modeled on the carboxy terminus of hirudin
    • (b) Jakubowski, J. A.; Maraganore, J. M. Inhibition of coagulation and thrombin induced platelet activities by a synthetic dodecapeptide modeled on the carboxy terminus of hirudin. Blood 1990, 75, 399-406.
    • (1990) Blood , vol.75 , pp. 399-406
    • Jakubowski, J.A.1    Maraganore, J.M.2
  • 11
    • 0025346345 scopus 로고
    • Design and characterization of hirulogs: A novel class of bivalent peptide inhibitors of thrombin
    • (c) Maraganore, J. M.; Bourdon, P.; Jablonski, J.; Ramachandran, K. L.; Fenton, J. W., II. Design and characterization of hirulogs: a novel class of bivalent peptide inhibitors of thrombin. Biochemistry 1990, 29, 7095-7101.
    • (1990) Biochemistry , vol.29 , pp. 7095-7101
    • Maraganore, J.M.1    Bourdon, P.2    Jablonski, J.3    Ramachandran, K.L.4    Fenton II, J.W.5
  • 12
    • 0027298337 scopus 로고
    • Design of a linker for trivalent thrombin inhibitors: Interaction of the main chain of the linker with thrombin
    • (d) Szewczuk, Z.; Gibbs, B. F.; Yue, S. Y.; Purisima, E.; Zdanov, A.; Cygler, M.; Konishi, Y. Design of a linker for trivalent thrombin inhibitors: interaction of the main chain of the linker with thrombin. Biochemistry 1993, 32, 3396-3404.
    • (1993) Biochemistry , vol.32 , pp. 3396-3404
    • Szewczuk, Z.1    Gibbs, B.F.2    Yue, S.Y.3    Purisima, E.4    Zdanov, A.5    Cygler, M.6    Konishi, Y.7
  • 13
    • 0028559927 scopus 로고
    • Design of potent bivalent thrombin inhibitors based on hirudin sequence: Incorporation of nonsubstrate-type active site inhibitors
    • (e) Tsuda, Y.; Cygler, M.; Gibbs, B. F.; Pedyczac, A.; Féthière, J.; Yue, S. Y.; Konishi, Y. Design of potent bivalent thrombin inhibitors based on hirudin sequence: incorporation of nonsubstrate-type active site inhibitors. Biochemistry 1994, 33, 14443-14451.
    • (1994) Biochemistry , vol.33 , pp. 14443-14451
    • Tsuda, Y.1    Cygler, M.2    Gibbs, B.F.3    Pedyczac, A.4    Féthière, J.5    Yue, S.Y.6    Konishi, Y.7
  • 14
    • 0022521744 scopus 로고
    • Kinetic of the inhibition of thrombin by hirudin
    • Stone, S. R.; Hofsteenge, J. Kinetic of the inhibition of thrombin by hirudin. Biochemistry 1986, 25, 4622-4628.
    • (1986) Biochemistry , vol.25 , pp. 4622-4628
    • Stone, S.R.1    Hofsteenge, J.2
  • 15
    • 0023203870 scopus 로고
    • Anticoagulant peptides: Nature of the interaction of the C-terminal region of hirudin with a noncatalytic binding site of thrombin
    • Krstenansky, J. L.; Owen, T. J.; Yates, M. T.; Mao, S. J. T. Anticoagulant peptides: nature of the interaction of the C-terminal region of hirudin with a noncatalytic binding site of thrombin. J. Med. Chem. 1987, 30, 1688-1691.
    • (1987) J. Med. Chem. , vol.30 , pp. 1688-1691
    • Krstenansky, J.L.1    Owen, T.J.2    Yates, M.T.3    Mao, S.J.T.4
  • 16
    • 0025866812 scopus 로고
    • Refined structure of the hirudin-thrombin complex
    • (a) Rydel, T. J.; Tulinsky, A.; Bode, W.; Huber, R. Refined structure of the hirudin-thrombin complex. J. Mol. Biol. 1991, 221, 583-601.
    • (1991) J. Mol. Biol. , vol.221 , pp. 583-601
    • Rydel, T.J.1    Tulinsky, A.2    Bode, W.3    Huber, R.4
  • 18
    • 0027366387 scopus 로고
    • Changes in interaction in complexes of hirudin derivatives and human α-thrombin due to different crystal forms
    • (c) Priestle, J. P.; Rahuel, J.; Rink, H.; Tones, M.; Grütter, M. G. Changes in interaction in complexes of hirudin derivatives and human α-thrombin due to different crystal forms. Protein Sci. 1993, 2, 1630-1642.
    • (1993) Protein Sci. , vol.2 , pp. 1630-1642
    • Priestle, J.P.1    Rahuel, J.2    Rink, H.3    Tones, M.4    Grütter, M.G.5
  • 21
    • 33947092515 scopus 로고
    • Structural basis of the activation and action of trypsin
    • (a) Huber, R.; Bode, W. Structural basis of the activation and action of trypsin. Acc. Chem. Res. 1978, 11, 114-122.
    • (1978) Acc. Chem. Res. , vol.11 , pp. 114-122
    • Huber, R.1    Bode, W.2
  • 22
    • 0003150431 scopus 로고
    • Introduction of protein inhibitors: X-ray crystallography
    • Elsevier: Amsterdam
    • (b) Read, R. J.; James, M. N. G. Introduction of protein inhibitors: X-ray crystallography. In Proteinase inhibitors; Elsevier: Amsterdam, 1986; pp 301-336.
    • (1986) Proteinase Inhibitors , pp. 301-336
    • Read, R.J.1    James, M.N.G.2
  • 23
    • 0028276982 scopus 로고
    • Retro-binding tripeptide thrombin active-site inhibitors: Discovery, synthesis, and molecular modeling
    • (a) Iwanowicz, E. J.; Lau, W. F.; Lin, J.; Roberts, D. G. M.; Seiler, S. M. Retro-binding tripeptide thrombin active-site inhibitors: discovery, synthesis, and molecular modeling. J. Med. Chem. 1994, 37, 2122-2124.
    • (1994) J. Med. Chem. , vol.37 , pp. 2122-2124
    • Iwanowicz, E.J.1    Lau, W.F.2    Lin, J.3    Roberts, D.G.M.4    Seiler, S.M.5
  • 25
    • 0027409404 scopus 로고
    • A player of many parts: The spotlight falls on thrombin structure
    • Stubbs, T. S.; Bode, W. A player of many parts: the spotlight falls on thrombin structure. Thrombosis Res. 1993, 69, 1-58.
    • (1993) Thrombosis Res. , vol.69 , pp. 1-58
    • Stubbs, T.S.1    Bode, W.2
  • 26
    • 0024431034 scopus 로고
    • The refined 1.9 A crystal structure of human α-thrombin: Interaction with D-Phe-Pro-Arg-chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment
    • Bode, W.; Mayr, I.; Baumann, U.; Huber, R.; Stone, S. R.; Hofsteenge, J. The refined 1.9 A crystal structure of human α-thrombin: interaction with D-Phe-Pro-Arg-chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment. EMBO J. 1989, 8, 3467-3475.
    • (1989) EMBO J. , vol.8 , pp. 3467-3475
    • Bode, W.1    Mayr, I.2    Baumann, U.3    Huber, R.4    Stone, S.R.5    Hofsteenge, J.6
  • 27
    • 0002943240 scopus 로고
    • Synthetic substrates and inhibitors of thrombin
    • Plenum Press: New York
    • Powers, J. C.; Kam, C.-M. Synthetic substrates and inhibitors of thrombin. In Thrombin: Structure and Function; Plenum Press: New York, 1992; pp 117-158.
    • (1992) Thrombin: Structure and Function , pp. 117-158
    • Powers, J.C.1    Kam, C.-M.2
  • 29
    • 0026074854 scopus 로고
    • Hirudin: Amino-terminal residues play a major role in the interaction with thrombin
    • Lazar, J. B.; Winant, R. C.; Johnson, P. H. Hirudin: Amino-terminal residues play a major role in the interaction with thrombin. J. Biol. Chem. 1991, 266, 685-688.
    • (1991) J. Biol. Chem. , vol.266 , pp. 685-688
    • Lazar, J.B.1    Winant, R.C.2    Johnson, P.H.3
  • 30
    • 0026633347 scopus 로고
    • Interaction of the N-terminal region of hirudin with the active-site cleft of thrombin
    • Betz, A.; Hosteenge, J.; Stone, S. R. Interaction of the N-terminal region of hirudin with the active-site cleft of thrombin. Biochemistry 1992, 31, 4557-4562.
    • (1992) Biochemistry , vol.31 , pp. 4557-4562
    • Betz, A.1    Hosteenge, J.2    Stone, S.R.3
  • 31
    • 0019231706 scopus 로고
    • Thrombin inhibitors. 3. Carboxyl-containing amide derivatives of Nα-substituted L-arginine
    • (a) Kikumoto, R.; Tamao, Y.; Ohkubo, K.; Tezuka, T.; Tonomura, S.; Okamoto, S.; Hijikata, A. Thrombin inhibitors. 3. Carboxyl-containing amide derivatives of Nα-substituted L-arginine. J. Med. Chem. 1980, 23, 1293-1299.
    • (1980) J. Med. Chem. , vol.23 , pp. 1293-1299
    • Kikumoto, R.1    Tamao, Y.2    Ohkubo, K.3    Tezuka, T.4    Tonomura, S.5    Okamoto, S.6    Hijikata, A.7
  • 32
    • 0023158165 scopus 로고
    • Studies of the pharmacodynamics of synthetic thrombin inhibitors of the basically substituted Na-aryl-sulfonylated phenylalanine amide type
    • (b) Kaiser, B.; Hauptman, J.; Markwardt, F. Studies of the pharmacodynamics of synthetic thrombin inhibitors of the basically substituted Na-aryl-sulfonylated phenylalanine amide type. Pharmazie 1987, 42, 119-121.
    • (1987) Pharmazie , vol.42 , pp. 119-121
    • Kaiser, B.1    Hauptman, J.2    Markwardt, F.3
  • 35
    • 0029147823 scopus 로고
    • Intrinsic φ, ψ propensities of amino acids, derived from coil regions of known structures
    • (b) Swindells, M. B.; MacArthur, M. W.; Thornton, J. M. Intrinsic φ, ψ propensities of amino acids, derived from coil regions of known structures. Nature Struct. Biol. 1995, 2, 596-603.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 596-603
    • Swindells, M.B.1    MacArthur, M.W.2    Thornton, J.M.3
  • 37
    • 0026502889 scopus 로고
    • Characterization of the interaction of a bifunctional inhibitor with α-thrombin by molecular modeling and peptide synthesis
    • Yue, S.-Y.; DiMaio, J.; Szewczuk, Z.; Purisima, E. O.; Ni, F.; Konishi, Y. Characterization of the interaction of a bifunctional inhibitor with α-thrombin by molecular modeling and peptide synthesis. Protein Eng. 1992, 5, 77-85.
    • (1992) Protein Eng. , vol.5 , pp. 77-85
    • Yue, S.-Y.1    DiMaio, J.2    Szewczuk, Z.3    Purisima, E.O.4    Ni, F.5    Konishi, Y.6
  • 38
    • 0025120271 scopus 로고
    • Use of fragments of hirudin to investigate thrombin-hirudin interaction
    • Dennis, S.; Wallace, A.; Hofsteenge, J.; Stone, S. R. Use of fragments of hirudin to investigate thrombin-hirudin interaction. Eur. J. Biochem. 1990, 188, 61-66.
    • (1990) Eur. J. Biochem. , vol.188 , pp. 61-66
    • Dennis, S.1    Wallace, A.2    Hofsteenge, J.3    Stone, S.R.4
  • 39
    • 0001926444 scopus 로고
    • Solid-Phase Peptide Synthesis
    • Gross, E., Meienhofer, J., Eds.; Academic Press: New York
    • Barany, G.; Merrifield, R. B. Solid-Phase Peptide Synthesis. In The Peptides: Analysis, Synthesis, Biology; Gross, E., Meienhofer, J., Eds.; Academic Press: New York, 1980; Vol. 2, pp 199-208.
    • (1980) The Peptides: Analysis, Synthesis, Biology , vol.2 , pp. 199-208
    • Barany, G.1    Merrifield, R.B.2
  • 40
    • 0025240978 scopus 로고
    • Development of MDL 28,050, a small antithrombin agent based on a functional domain of the leech protein, hirudin
    • Krstenansky, J. L.; Broersma, R. J.; Owen, T. J.; Payne, M. H.; Yates, M. T.; Mao, S. J. Development of MDL 28,050, a small antithrombin agent based on a functional domain of the leech protein, hirudin. Thromb. Haemostasis 1990, 63, 208-214.
    • (1990) Thromb. Haemostasis , vol.63 , pp. 208-214
    • Krstenansky, J.L.1    Broersma, R.J.2    Owen, T.J.3    Payne, M.H.4    Yates, M.T.5    Mao, S.J.6
  • 41
    • 0026786833 scopus 로고
    • Conformationally restricted thrombin inhibitors resistant to proteoplytic digestion
    • (a) Szewczuk, Z.; Gibbs, B. F.; Yue, S.-Y.; Purisima, E. O.; Konishi, Y. Conformationally restricted thrombin inhibitors resistant to proteoplytic digestion. Biochemistry 1992, 31, 9132-9140.
    • (1992) Biochemistry , vol.31 , pp. 9132-9140
    • Szewczuk, Z.1    Gibbs, B.F.2    Yue, S.-Y.3    Purisima, E.O.4    Konishi, Y.5
  • 42
    • 0023723033 scopus 로고
    • Design, synthesis and antithrombin activity for conformationally restricted analogs of peptide anticoagulants based on the C-terminal region of the leech peptide, hirudin
    • (b) Krstenansky, J. L.; Owen, T. J.; Yates, M. T.; Mao, S. J. T. Design, synthesis and antithrombin activity for conformationally restricted analogs of peptide anticoagulants based on the C-terminal region of the leech peptide, hirudin. Biochim. Biophys. Acta 1988, 957, 53-59.
    • (1988) Biochim. Biophys. Acta , vol.957 , pp. 53-59
    • Krstenansky, J.L.1    Owen, T.J.2    Yates, M.T.3    Mao, S.J.T.4
  • 43
    • 0028166473 scopus 로고
    • Thrombin-bound conformation of a cyclic anticoagulant peptide using transferred nuclear Overhauser effect (NOE), distance geometry, and NOE simulations
    • (c) Ning, Q.; Ripoll, D. R.; Szewczuk, Z.; Konishi, Y.; Ni, F. Thrombin-bound conformation of a cyclic anticoagulant peptide using transferred nuclear Overhauser effect (NOE), distance geometry, and NOE simulations. Biopolymers 1994, 34, 1125-1137.
    • (1994) Biopolymers , vol.34 , pp. 1125-1137
    • Ning, Q.1    Ripoll, D.R.2    Szewczuk, Z.3    Konishi, Y.4    Ni, F.5
  • 46
    • 0021024613 scopus 로고
    • The functional domain of hirudin, a thrombin-specific inhibitor
    • (b) Chang, J.-Y. The functional domain of hirudin, a thrombin-specific inhibitor. FEBS Lett. 1983, 164, 307-313.
    • (1983) FEBS Lett. , vol.164 , pp. 307-313
    • Chang, J.-Y.1
  • 47
    • 0025614350 scopus 로고
    • Production, properties, and thrombin inhibitory mechanism of hirudin amino-terminal core fragments
    • (c) Chang, J.-Y. Production, properties, and thrombin inhibitory mechanism of hirudin amino-terminal core fragments. J. Biol. Chem. 1990, 265, 22159-22166.
    • (1990) J. Biol. Chem. , vol.265 , pp. 22159-22166
    • Chang, J.-Y.1
  • 57
    • 33644787399 scopus 로고
    • Consistent force field studies of intermolecular forces in hydrogen bonded crystals. 1. carboxylic acids, amides and the C-OH hydrogen bonds
    • (a) Lifson, S.; Hagler, A. T.; Dauber, P. Consistent force field studies of intermolecular forces in hydrogen bonded crystals. 1. carboxylic acids, amides and the C-OH hydrogen bonds. J. Am. Chem. Soc. 1979, 101, 5111-5121.
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 5111-5121
    • Lifson, S.1    Hagler, A.T.2    Dauber, P.3
  • 58
    • 33845560932 scopus 로고
    • Consistent force field studies of intermolecular forces in hydrogen bonded crystals. 2. a banchmark for the objective comparison of alternative force field
    • (b) Hagler, A. T.; Dauber, P.; Lifson, S. Consistent force field studies of intermolecular forces in hydrogen bonded crystals. 2. a banchmark for the objective comparison of alternative force field. J. Am. Chem. Soc. 1979, 101, 5131-5141.
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 5131-5141
    • Hagler, A.T.1    Dauber, P.2    Lifson, S.3
  • 59
    • 6344256147 scopus 로고
    • Consistent force field studies of intermolecular forces in hydrogen bonded crystals. 3. the C=OH-O hydrogen bond and the analysis of the energetics and packing of carboxylic acids
    • (c) Hagler, A. T.; Lifson, S.; Dauber, P. Consistent force field studies of intermolecular forces in hydrogen bonded crystals. 3. the C=OH-O hydrogen bond and the analysis of the energetics and packing of carboxylic acids. J. Am. Chem. Soc. 1979, 101, 5122-5130.
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 5122-5130
    • Hagler, A.T.1    Lifson, S.2    Dauber, P.3
  • 60
    • 0026010908 scopus 로고
    • PyBOP and PyBroP: Two reagents for the difficult coupling of the α,α-dialkyl amino acid, Aib
    • Frérot, E.; Coste, J.; Pantaloni, A.; Dufour, M. N.; Jouin, P. PyBOP and PyBroP: two reagents for the difficult coupling of the α,α-dialkyl amino acid, Aib. Tetrahedron 1991, 47, 259-270.
    • (1991) Tetrahedron , vol.47 , pp. 259-270
    • Frérot, E.1    Coste, J.2    Pantaloni, A.3    Dufour, M.N.4    Jouin, P.5
  • 61
    • 0014772602 scopus 로고
    • Color test for detection of free terminal amino groups in the solid-phase synthesis of peptides
    • Kaiser, E.; Colescott, R. L.; Bossinger, C. D.; Cook, P. I. Color test for detection of free terminal amino groups in the solid-phase synthesis of peptides. Anal. Biochem. 1970, 34, 595-598.
    • (1970) Anal. Biochem. , vol.34 , pp. 595-598
    • Kaiser, E.1    Colescott, R.L.2    Bossinger, C.D.3    Cook, P.I.4
  • 64
    • 0003518480 scopus 로고
    • J. Wiley & Sons: New York
    • Segel, I. H. In Enzyme Kinetics; J. Wiley & Sons: New York, 1975.
    • (1975) Enzyme Kinetics
    • Segel, I.H.1


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