Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/337505
Type: Artigo
Title: The self-assembling peptide P-11-4 prevents collagen proteolysis in dentin
Author: de Sousa, J. P.
Carvalho, R. G.
Barbosa-Martins, L. F.
Torquato, R. J. S.
Mugnol, K. C. U.
Nascimento, F. D.
Tersariol, I. L. S.
Puppin-Rontani, R. M.
Abstract: The major goal in restorative dentistry is to develop a true regenerative approach that fully recovers hydroxyapatite crystals within the caries lesion. Recently, a rationally designed self-assembling peptide P-11-4 (Ace-QQRFEWEFEQQ-NH2) has been developed to enhance remineralization on initial caries lesions, yet its applicability on dentin tissues remains unclear. Thus, the present study investigated the interaction of P-11-4 with the organic dentin components as well as the effect of P-11-4 on the proteolytic activity, mechanical properties of the bonding interface, and nanoleakage evaluation to artificial caries-affected dentin. Surface plasmon resonance and atomic force microscopy indicated that P-11-4 binds to collagen type I fibers, increasing their width from 214 +/- 4 nm to 308 +/- 5 nm (P < 0.0001). P-11-4 also increased the resistance of collagen type I fibers against the proteolytic activity of collagenases. The immediate treatment of artificial caries-affected dentin with P-11-4 enhanced the microtensile bonding strength of the bonding interface (P < 0.0001), reaching values close to sound dentin and decreasing the proteolytic activity at the hybrid layer; however, such effects decreased after 6 mo of water storage (P < 0.05). In conclusion, P-11-4 interacts with collagen type I, increasing the resistance of collagen fibers to proteolysis, and improves stability of the hybrid layer formed by artificial caries-affected dentin
Subject: Biomateriais
Country: Estados Unidos
Editor: Sage
Rights: Fechado
Identifier DOI: 10.1177/0022034518817351
Address: https://journals.sagepub.com/doi/10.1177/0022034518817351
Date Issue: 2019
Appears in Collections:FOP - Artigos e Outros Documentos

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