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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Chlorhexidine Inhibits the Activity of Dental Cysteine Cathepsins

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Scaffa, P. M. C. [1] ; Vidal, C. M. P. [1] ; Barros, N. [2] ; Gesteira, T. F. [3] ; Carmona, A. K. [2] ; Breschi, L. [4, 5, 6] ; Pashley, D. H. [7] ; Tjaderhane, L. [8, 9] ; Tersariol, I. L. S. [3, 10] ; Nascimento, F. D. [11] ; Carrilho, M. R. [11]
Total Authors: 11
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[1] Univ Estadual Campinas, Piracicaba Dent Sch, Dept Restorat Dent, Piracicaba - Brazil
[2] Univ Fed Sao Paulo, Dept Biophys, Sao Paulo - Brazil
[3] Univ Fed Sao Paulo, Dept Biochem, Sao Paulo - Brazil
[4] Univ Trieste, Dept Biomed, Bologna - Italy
[5] IGM CNR, Bologna - Italy
[6] IOR, Unit Bologna, Bologna - Italy
[7] Georgia Hlth Sci Univ, Coll Dent Med, Dept Oral Biol, Augusta, GA - USA
[8] Univ Oulu, Inst Dent, Oulu - Finland
[9] Oulu Univ Hosp, Oulu - Finland
[10] Univ Mogi das Cruzes, Ctr Interdisciplinar Invest Bioquim, Mogi das Cruzes - Brazil
[11] Univ Bandeirante Sao Paulo, Biomat Res Grp, BR-02071013 Sao Paulo - Brazil
Total Affiliations: 11
Document type: Journal article
Source: JOURNAL OF DENTAL RESEARCH; v. 91, n. 4, p. 420-425, APR 2012.
Web of Science Citations: 107

The co-expression of MMPs and cysteine cathepsins in the human dentin-pulp complex indicates that both classes of enzymes can contribute to the endogenous proteolytic activity of dentin. Chlorhexidine (CHX) is an efficient inhibitor of MMP activity. This study investigated whether CHX could also inhibit cysteine cathepsins present in dentin. The inhibitory profile of CHX on the activity of dentin-extracted and recombinant cysteine cathepsins (B, K, and L) was monitored in fluorogenic substrates. The rate of substrate hydrolysis was spectrofluorimetrically measured, and inhibitory constants were calculated. Molecular docking was performed to predict the binding affinity between CHX and cysteine cathepsins. The results showed that CHX inhibited the proteolytic activity of dentin-extracted cysteine cathepsins in a dose-dependent manner. The proteolytic activity of human recombinant cathepsins was also inhibited by CHX. Molecular docking analysis suggested that CHX strongly interacts with the subsites S2 to S2' of cysteine cathepsins B, K, and L in a very similar manner. Taken together, these results clearly showed that CHX is a potent inhibitor of the cysteine cathepsins-proteolytic enzymes present in the dentin-pulp complex. (AU)

FAPESP's process: 09/14005-9 - Effect of protease inhibitors on the solubilization of demineralized dentin, preservation of mechanical properties of dentin matrix and durability of adhesive restorations.
Grantee:Polliana Mendes Candia Scaffa
Support type: Scholarships in Brazil - Doctorate
FAPESP's process: 11/12226-8 - Activity of host-derived proteases on degradation of human dentin treated for bonding procedures
Grantee:Marcela Rocha de Oliveira Carrilho
Support type: Scholarships abroad - Research