Chromogenic substrates as fundamental tool to design new thrombin inhibitors: Determination of inhibition equilibrium constants

Hamostaseologie

Volumn 25, Issue 3, 2005, Pages 267-271

  López, Mercedes ^a   Nowak, G ^b  

^a INSTITUTO VENEZOLANO DE INVESTIGACIONES CIENTÍFICAS   (Venezuela)

^b FRIEDRICH SCHILLER UNIVERSITY JENA   (Germany)

Author keywords

Chromogenic thrombin substrate; Direct thrombin inhibitor; Ki value

Indexed keywords

CHROMOGENIC SUBSTRATE; COMPLEMENTARY DNA; DEXTRO PHENYLALANYLPIPECOLYLARGININE 4 NITROANILIDE; DIPETALOGASTIN II; DIPETARUDIN; HIRUDIN; THROMBIN; THROMBIN INHIBITOR; UNCLASSIFIED DRUG;

CHIMERA; DRUG DESIGN; EQUILIBRIUM CONSTANT; MOLECULAR CLONING; MOLECULAR WEIGHT; POLYMERASE CHAIN REACTION; REVIEW; STRUCTURE ACTIVITY RELATION;

EID: 23944520677     PISSN: 07209355     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-0037-1619660     Document Type: Review

References (17)

1. Fuentes-Prior P, Noeske-Jungblut C, Donner P et al. Structure of the thrombin complex with triabin, a lipocalin-like exosite-binding inhibitor derived from a triatomine bug. Proc Natl Acad Sci USA 1997; 94: 11845-50.
2. Grütter M, Priestle J, Rahuel J. Crystal structure of the thrombin-hirudin complex: a novel mode of serine protease inhibition. EMBO J 1990; 9: 2361-5.
3. Lange U, Keilholz W, Schaub G et al. Biochemical characterization of a thrombin inhibitor from the bloodsucking bug Dipetalogaster maximus. Haemostasis 1999; 29: 204-11.
4. López M, Mende K, Steinmetzer T et al. Cloning, purification and biochemical characterization of dipetarudin, a new chimeric thrombin inhibitor. J Chrom B 2003; 786: 73-80.
5. Maraganore J, Bourdon P, Jablonski J et al. Design and characterization of hirulogs: a novel class of bivalent peptide inhibitors of thrombin. Biochemistry 1990; 29: 7095-101.
6. Markwardt F. Die Isolierung und chemische Charakterisierung des Hirudins. Z Physiol Chem 1957; 312: 85-9.
7. Mende K, Petoukhova O, Koulitchkova V et al. Dipetalogastin, a potent thrombin inhibitor from the blood-sucking insect Dipetalogaster maximus. Eur J Biochem 1999; 266: 583-90.
8. Morrison J, Stone S. Approaches to the study and analysis of the inhibition of enzymes by slow and tight binding inhibitors. Comm Mol Cell Biophys 1995; 2: 347-68.
9. Morrison J, Walsh C. The behavior and significance of slow-binding enzyme inhibitors. Adv Enzymol 1988; 61: 201-301.
10. Morrison J. Kinetics of the reversible inhibition of enzyme-catalysed reactions by tight-binding inhibitors. Biochim Biophys Acta 1969; 185: 269-86.
11. nd, Maraganore J et al. The COOH-terminal domain of hirudin. An exosite-directed competitive inhibitor of the action of alpha-thrombin on fibrinogen. J Biol Chem 1990; 265: 13484-9.
12. Richardson J, Kröger B, Hoeffken W et al. Crystal structure of the human αcomplex: an exosite II-binding inhibitor. EMBO J 2000; 19: 5650-60.
13. Rydel T, Ravichandran K, Tulinsky A et al. The structure of a complex of recombinant hirudin and human alpha-thrombin. Science 1990; 249: 277-80.
14. Stone S, Hofsteenge J. Kinetics of the inhibition of thrombin by hirudin. Biochemistry 1986; 25: 4622-8.
15. van de Locht A, Lamba D, Bauer M et al. Two heads are better than one: crystal structure of the insect derived double domain Kazal inhibitor rhodniin in complex with thrombin. EMBO J 1995; 14: 5149-57.
16. van de Locht A, Stubbs M, Bode W et al. The ornithodorin-thrombin crystal structure, a key to the TAP enigma? EMBO J 1996; 15: 6011-7.
17. Williams J, Morrison J. The kinetics of reversible tight-binding inhibition. Meth Enzymol 1979; 63: 437-67.