From natural to synthetic multisite thrombin inhibitors
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From natural to synthetic multisite thrombin inhibitors (452 views)

Lombardi A, De Simone G, Galdiero S, Staiano N, Nastri F, Pavone V

Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1999; 51(1): 19-39.

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Paper type: Journal Article,

Impact factor: 2.331, 5-year impact factor: 2.594

Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-0033041934&partnerID=40&md5=f5f3ea399a7ab9c7ae417e72bca4c6bb

Keywords: Antithrombotics, Hirunorms, Multisite Directed Thrombin-Inhibitors, Natural Thrombin Inhibitors, X-Ray Crystal Structures, Agents, Catalyst Activity, Drug Products, Molecular Structure, X Ray Crystallography, Enzyme Inhibition, Antithrombin Iii, Argatroban, Cyclotheonamide A, Dansylarginyl Dextro Pipercolic Acid, Hirulog, Mdl 28050, Nazumamide A, Ornithodorin, Triabin, Unclassified Drug, Anticoagulation, Article, Drug Conformation, Drug Isolation, Drug Protein Binding, Enzyme Active Site, Leech, Sponge (porifera), Structure Activity Relation, Amino Acid Sequence, Animals, Binding Sites, Drug Design, Fibrinogen, Hirudins, Humans, Models, Molecular Sequence Data, Protein Conformation, Serine Proteinase Inhibitors, Hirudinida,

Affiliations:
Ctro. Interuniversitario di R., Ctr. di Stud. di B., University of Napoli Federico II, via Mezzocannone 4, 80134, Napoli, Italy
Dipto. di Biochim. e B., University of Napoli Federico II, via Pansini 5, 80129 Napoli, Italy


References:
Not available.
From natural to synthetic multisite thrombin inhibitors

A large number of potent and selective therapeutic agents, useful for the treatment of several diseases, have been isolated from natural sources. For example, the most active thrombin inhibitors are those secreted by the salivary glands of leeches. One peculiar feature of these agents is the lack of any significant inhibitory cross-reaction with other serine proteinases. Hence, the knowledge of the exact mechanism of action of these molecules provides the basis for the development of new and efficient synthetic drugs. For this reason, many studies have been undertaken on the structure-activity relationships of natural thrombin inhibitors, and a large amount of detailed information has been obtained by the crystal structures of these inhibitors when complexed with thrombin. In this paper, we review natural and synthetic multisite thrombin inhibitors, whose structural aspects have been determined in detail. We also report here the approach used by us to develop a new class of synthetic, multisite directed thrombin inhibitors, named hirunorms, designed to mimic the distinctive binding mode of hirudin.
From natural to synthetic multisite thrombin inhibitors

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From natural to synthetic multisite thrombin inhibitors

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Vitale R, Lista L, Cerrone C, Caserta G, Chino M, Maglio O, Nastri F, Pavone V, Lombardi A
* An artificial heme-enzyme with enhanced catalytic activity: evolution, functional screening and structural characterization (571 views)
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Impact Factor: 3.559
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Nastri F, Lista L, Ringhieri P, Vitale R, Faiella M, Andreozzi C, Travascio P, Maglio O, Lombardi A, Pavone V
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Impact Factor: 5.925
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Bonomo RP, Bruno V, Conte E, De Guidi G, La Mendola D, Maccarrone G, Nicoletti F, Rizzarelli E, Sortino S, Vecchio G
* Potentiometric, spectroscopic and antioxidant activity studies of SOD mimics containing carnosine (449 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2003; (23): 4406-4415.
Impact Factor: 2.908
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Pavone V, De Simone G, Nastri F, Galdiero S, Staiano N, Lombardi A, Pedone C
Multiple binding mode of reversible synthetic thrombin inhibitors. A comparative structural analysis (683 views)
Biol Chem Biological Chemistry (ISSN: 1431-6730, 1437-4315), 1998 Sep; 379(8-9): 987-1006.
Impact Factor: 2.636
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De Simone G, Lombardi A, Galdiero S, Nastri F, Della Morte R, Staiano N, Pedone C, Bolognesi M, Pavone V
Hirunorms Are True Hirudin Mimetics. The Crystal Structure Of Human Alpha-Thrombin-Hirunorm V Complex (698 views)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 1998 Feb; 7(2): 243-253.
Impact Factor: 4.44
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Pavone V, Lombardi A, Saviano M, Di Blasio B, Nastri F, Fattorusso R, Zaccaro L, Maglio O, Yamada T, Omote Y
Mixed conformation in C(α, α)-disubstituted tripeptides: X-ray crystal structures of Z-Aib-Dph-Gly-OMe and Bz-Dph-Dph-Gly-OMe (448 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1994 Dec; 34(12): 1595-1604.
Impact Factor: 2.425
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6 Records (6 excluding Abstracts).
Total impact factor: 21.893 (21.893 excluding Abstracts).
Total 5 year impact factor: 22.388 (22.388 excluding Abstracts).

Last modified by Marco Comerci on Sunday 12 July 2020, 13:15:14
452 views. Last view on Saturday 01 June 2024, 5:49:25