From natural to synthetic multisite thrombin inhibitors (349 views)
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
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Witting, J. I., Bourdon, P., Brezniak, D. V., Maraganore, J. M., Fenton J. W. II, (1992) Biochem J, 283, pp. 737-743
Read, R. J., James, M. N. G., (1986) Protein Inhibitors, pp. 301-336. , Barret, A. J., Salven, E. Eds.
F thi re, J., Tsuda, Y., Coulombe, R., Konishi, Y., Cygler, M., (1996) Protein Sci, 5, pp. 1174-1183
Banner, D. W., Hadvary, P., (1991) J Biol Chem, 266, pp. 20085-20093
Rehse, P. H., Steinmetzer, T., Li, Y., Konishi, Y., Cygler, M., (1995) Biochemistry, 34, pp. 11537-11544
Abola, E. E., Sussman, J. L., Prilusky, J., Manning, N. O., (1997) Methods Enzymol, 277, pp. 556-571
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1999; 51(1): 19-39.
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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
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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.
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 (447 views)
Org Biomol Chem (ISSN: 1477-0520, 1477-0539, 1477-0539electronic), 2015 Apr 22; 13(17): 4859-4868.
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
* A Heme-Peptide Metalloenzyme Mimetic with Natural Peroxidase-Like Activity (435 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2011 Apr; 17(16): 4444-4453.
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 (385 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 (589 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 (520 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 (400 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1994 Dec; 34(12): 1595-1604.
Impact Factor: 2.425
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* An artificial heme-enzyme with enhanced catalytic activity: evolution, functional screening and structural characterization (447 views)
Org Biomol Chem (ISSN: 1477-0520, 1477-0539, 1477-0539electronic), 2015 Apr 22; 13(17): 4859-4868.
Impact Factor: 3.559
View Export to BibTeX Export to EndNote
Nastri F, Lista L, Ringhieri P, Vitale R, Faiella M, Andreozzi C, Travascio P, Maglio O, Lombardi A, Pavone V
* A Heme-Peptide Metalloenzyme Mimetic with Natural Peroxidase-Like Activity (435 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2011 Apr; 17(16): 4444-4453.
Impact Factor: 5.925
View Export to BibTeX Export to EndNote
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 (385 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2003; (23): 4406-4415.
Impact Factor: 2.908
View Export to BibTeX Export to EndNote
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 (589 views)
Biol Chem Biological Chemistry (ISSN: 1431-6730, 1437-4315), 1998 Sep; 379(8-9): 987-1006.
Impact Factor: 2.636
View Export to BibTeX Export to EndNote
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 (520 views)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 1998 Feb; 7(2): 243-253.
Impact Factor: 4.44
View Export to BibTeX Export to EndNote
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 (400 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1994 Dec; 34(12): 1595-1604.
Impact Factor: 2.425
View Export to BibTeX Export to EndNote
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).
Total impact factor: 21.893 (21.893 excluding Abstracts).
Total 5 year impact factor: 22.388 (22.388 excluding Abstracts).
349 views. Last view on Saturday 14 January 2023, 17:41:52
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