A thermodynamic characterization of the binding of thrombin inhibitors to human thrombin, combining biosensor technology, stopped-flow spectrophotometry, and microcalorimetry

Analytical Biochemistry

Volumn 300, Issue 2, 2002, Pages 152-162

  Deinum, Johanna ^a   Gustavsson, Lars ^a   Gyzander, Erika ^a   Kullman Magnusson, Mari ^b   Edström, Åsa ^b   Karlsson, Robert ^b  

^a ASTRAZENECA R AND D   (Sweden)

^b BIACORE AB   (Sweden)

Author keywords

Progress phase analysis; Serine protease inhibitor; Surface plasmon resonance; Thermodynamics

Indexed keywords

AMINO ACIDS; CALORIMETERS; CHEMICAL ANALYSIS; DISSOCIATION; EQUILIBRIUM CONSTANTS; PLASMONS; RATE CONSTANTS; SPECTROPHOTOMETRY; SURFACE PLASMON RESONANCE; TEMPERATURE; THERMODYNAMICS;

DISSOCIATION RATE CONSTANT; INHIBITION CONSTANTS; ISOTHERMAL TITRATION MICROCALORIMETRY; PHASE ANALYSIS; SERINE PROTEASE INHIBITOR; STOPPED-FLOW SPECTROPHOTOMETRY; THERMODYNAMIC CHARACTERIZATION; THROMBIN INHIBITORS;

ENZYMES;

CH 248; INOGATRAN; MELAGATRAN; THROMBIN; THROMBIN INHIBITOR; UNCLASSIFIED DRUG;

ARTICLE; BINDING KINETICS; BIOSENSOR; CHEMICAL COMPOSITION; CORRELATION ANALYSIS; CRYSTALLIZATION; DISSOCIATION CONSTANT; DRUG PROTEIN BINDING; ENTHALPY; EQUILIBRIUM CONSTANT; HUMAN; INHIBITION KINETICS; MATHEMATICAL ANALYSIS; MATHEMATICAL COMPUTING; MICROCALORIMETRY; MOLECULAR STABILITY; MOLECULAR WEIGHT; PRIORITY JOURNAL; PROTEIN IMMOBILIZATION; SPECTROPHOTOMETRY; SURFACE PLASMON RESONANCE; TEMPERATURE SENSITIVITY; THERMODYNAMICS; TITRIMETRY;

EID: 0037081320     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1006/abio.2001.5454     Document Type: Article

References (21)

1. The mechanism of binding of low-molecular-weight active site inhibitors to human alpha-thrombin
2. Biosensor analysis of drug-target interactions: Direct and competitive binding assays for investigation of interactions between thrombin and thrombin inhibitors
3. Affinity analysis of non-steady-state data obtained under mass transport limited conditions using BIAcore technology
4. The importance of enzyme inhibition kinetics for the effect of thrombin inhibitors in a rat model of arterial thrombosis
5. Thrombin inhibitors as antithrombotic agents: The importance of rapid inhibition
6. Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors
7. Quantitative determination of surface concentration of protein with surface plasmon resonance by using radiolabelled proteins
8. Kinetic analysis of the interaction between HIV-1 protease and inhibitors using optical biosensor technology
9. Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system
10. Kinetic and concentration analysis using BIA technology
11. Experimental design for kinetic analysis of protein-protein interactions with surface plasmon resonance biosensors
12. Thrombin inhibition by hirudin: How hirudin inhibits thrombin
13. The action of thrombin on peptide p-nitroanilide substrates
14. The behavior and significance of slow-binding enzyme inhibitors
15. Tight-binding inhibitors. III. A new approach for the determination of competition between tight-binding inhibitors and substrates - Inhibition of adenosine deaminase by coformycin
16. Thermodynamics of substrates and reversible inhibitors binding to the active site cleft of human alpha-thrombin
17. Significant discrepancies between van't Hoff and calorimetric enthalpies
18. Kinetic analysis of a protein antigen-antibody interaction limited by mass transport on an optical biosensor
19. Thermodynamic analysis of protein interactions with biosensor technology
20. TCR binding to peptide-MHC stabilizes a flexible recognition interface