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Type: Artigo de periódico
Title: Chlorhexidine Inhibits the Activity of Dental Cysteine Cathepsins
Author: Scaffa, PMC
Vidal, CMP
Barros, N
Gesteira, TF
Carmona, AK
Breschi, L
Pashley, DH
Tjaderhane, L
Tersariol, ILS
Nascimento, FD
Carrilho, MR
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.
Subject: cysteine cathepsins
proteolytic activity
Country: EUA
Editor: Sage Publications Inc
Rights: fechado
Identifier DOI: 10.1177/0022034511435329
Date Issue: 2012
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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