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Chlorhexidine inhibits the activity of dental cysteine cathepsins. (Articolo in rivista)

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Chlorhexidine inhibits the activity of dental cysteine cathepsins. (Articolo in rivista) (literal)

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Scaffa PM, Vidal CM, Barros N, Gesteira TF, Carmona AK, Breschi L, Pashley DH, Tjäderhane L, Tersariol IL, Nascimento FD, Carrilho MR. (2012)
Chlorhexidine inhibits the activity of dental cysteine cathepsins.
in Journal of dental research
(literal)

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Scaffa PM, Vidal CM, Barros N, Gesteira TF, Carmona AK, Breschi L, Pashley DH, Tjäderhane L, Tersariol IL, Nascimento FD, Carrilho MR. (literal)

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Department of Restorative Dentistry, Piracicaba Dental School, State University of Campinas, Piracicaba, Brazil; Department of Biophysics, Federal University of Sao Paulo, Sao Paulo, Brazil; Department of Biochemistry, Federal University of Sao Paulo, Sao Paulo, Brazil; Department of Biomedicine, University of Trieste, and IGM-CNR and Unit of Bologna c/o IOR, Bologna, Italy; Department of Oral Biology, College of Dental Medicine, Georgia Health Sciences University, Augusta, GA, USA; Institute of Dentistry, University of Oulu and Oulu University Hospital, Oulu, Finland; Centro Interdisciplinar de Investig. Bioquimica, University of Mogi das Cruzes, Mogi das Cruzes, Brazil; Biomaterials Research Group, Bandeirante University of Sao Paulo, Rua Maria Candida, 1813, 6 andar, Sao Paulo, 02071-013, Brazil (literal)

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Abstract

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. (literal)

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