Literature DB >> 8296393

Synthetic low-molecular weight thrombin inhibitors: molecular design and pharmacological profile.

C Tapparelli1, R Metternich, C Ehrhardt, N S Cook.   

Abstract

Thrombin is a multifunctional protein: in addition to its role in coagulation, thrombin has important biological effects on platelets, endothelial and smooth muscle cells, leukocytes, the heart and neurones. A detailed understanding of the structure of thrombin, of related serine proteases and of enzyme-inhibitor complexes has aided in the discovery of potent and selective new inhibitor molecules. Some of these novel thrombin inhibitors are active when administered orally and have shown remarkable efficacy as antithrombotic agents in animal models, offering a greater therapeutic potential than presently available drugs. This potential extends also to non-thrombotic indications where thrombin may be involved, namely inflammation, cancer and neurodegenerative diseases. The recent identification of specific thrombin receptors on different cells provides an alternative strategy for inhibiting thrombin's cellular actions, without necessarily compromising its role in haemostasis. In this review, Carlo Tapparelli and colleagues present a comprehensive update of these recent developments in the field of thrombin biology and pharmacology suggesting a new era of therapeutic drugs is on the horizon.

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Year:  1993        PMID: 8296393     DOI: 10.1016/0165-6147(93)90095-2

Source DB:  PubMed          Journal:  Trends Pharmacol Sci        ISSN: 0165-6147            Impact factor:   14.819


  17 in total

1.  Improvement of the intestinal absorption of a peptidomimetic, boronic acid thrombin inhibitor possibly utilizing the oligopeptide transporter.

Authors:  H Saitoh; B J Aungst
Journal:  Pharm Res       Date:  1999-11       Impact factor: 4.200

2.  Computer based screening of compound databases: 1. Preselection of benzamidine-based thrombin inhibitors.

Authors:  T Fox; E E Haaksma
Journal:  J Comput Aided Mol Des       Date:  2000-07       Impact factor: 3.686

3.  Structural basis for chemical inhibition of human blood coagulation factor Xa.

Authors:  K Kamata; H Kawamoto; T Honma; T Iwama; S H Kim
Journal:  Proc Natl Acad Sci U S A       Date:  1998-06-09       Impact factor: 11.205

4.  Computational combinatorial ligand design: application to human alpha-thrombin.

Authors:  A Caflisch
Journal:  J Comput Aided Mol Des       Date:  1996-10       Impact factor: 3.686

5.  Functionality map analysis of the active site cleft of human thrombin.

Authors:  P D Grootenhuis; M Karplus
Journal:  J Comput Aided Mol Des       Date:  1996-02       Impact factor: 3.686

6.  Incorporation of noncoded amino acids into the N-terminal domain 1-47 of hirudin yields a highly potent and selective thrombin inhibitor.

Authors:  V De Filippis; I Russo; A Vindigni; E Di Cera; S Salmaso; A Fontana
Journal:  Protein Sci       Date:  1999-10       Impact factor: 6.725

7.  The crystal structure of alpha-thrombin-hirunorm IV complex reveals a novel specificity site recognition mode.

Authors:  A Lombardi; G De Simone; F Nastri; S Galdiero; R Della Morte; N Staiano; C Pedone; M Bolognesi; V Pavone
Journal:  Protein Sci       Date:  1999-01       Impact factor: 6.725

8.  YD-3, a novel inhibitor of protease-induced platelet activation.

Authors:  C C Wu; S W Huang; T L Hwang; S C Kuo; F Y Lee; C M Teng
Journal:  Br J Pharmacol       Date:  2000-07       Impact factor: 8.739

9.  The effects of stimulating protease-activated receptor-1 and -2 in A172 human glioblastoma.

Authors:  T Okamoto; M Nishibori; K Sawada; H Iwagaki; N Nakaya; A Jikuhara; N Tanaka; K Saeki
Journal:  J Neural Transm (Vienna)       Date:  2001       Impact factor: 3.575

10.  Protease-activated receptor (PAR)-independent growth and pro-inflammatory actions of thrombin on human cultured airway smooth muscle.

Authors:  Thai Tran; Alastair G Stewart
Journal:  Br J Pharmacol       Date:  2003-03       Impact factor: 8.739

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