Chlorhexidine Inhibits the Activity of Dental Cysteine Cathepsins

Autor(es):Mostrar menos -

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]

Afiliação do(s) autor(es):Mostrar menos -

^[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

• Tipo de documento: Artigo Científico
• Fonte: JOURNAL OF DENTAL RESEARCH; v. 91, n. 4, p. 420-425, APR 2012.
• Citações Web of Science: 107

Resumo

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)

• Processo FAPESP: 07/54618-4 - Avaliação da atividade de colagenases na degradação da dentina humana tratada por procedimentos restauradores adesivos
• Beneficiário: Marcela Rocha de Oliveira Carrilho
• Modalidade de apoio: Auxílio à Pesquisa - Jovens Pesquisadores
• Processo FAPESP: 09/14005-9 - Efeito de inibidores de protease na solubilização da dentina desmineralizada, na preservação das propriedades mecânicas da matriz de dentina e na durabilidade das restaurações adesivas.
• Beneficiário: Polliana Mendes Candia Scaffa
• Modalidade de apoio: Bolsas no Brasil - Doutorado
• Processo FAPESP: 11/12226-8 - Avaliação da atividade de proteases na degradação da dentina humana tratada por procedimentos restauradores adesivos
• Beneficiário: Marcela Rocha de Oliveira Carrilho
• Modalidade de apoio: Bolsas no Exterior - Pesquisa