The Self-Assembling Peptide P-11-4 Prevents Collag... - BV FAPESP
Advanced search
Start date
Betweenand
(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

The Self-Assembling Peptide P-11-4 Prevents Collagen Proteolysis in Dentin

Full text
Author(s):
de Sousa, J. P. [1] ; Carvalho, R. G. [2] ; Barbosa-Martins, L. F. [1] ; Torquato, R. J. S. [2] ; Mugnol, K. C. U. [3] ; Nascimento, F. D. [3] ; Tersariol, I. L. S. [2] ; Puppin-Rontani, R. M. [1]
Total Authors: 8
Affiliation:
[1] Univ Estadual Campinas, Piracicaba Dent Sch, Dept Pediat Dent, Campinas, SP - Brazil
[2] Univ Fed Sao Paulo, Dept Biochem, Sao Paulo, SP - Brazil
[3] Univ Mogi das Cruzes, Interdisciplinary Ctr Biochem Invest, BR-08773520 Mogi Das Cruzes, SP - Brazil
Total Affiliations: 3
Document type: Journal article
Source: JOURNAL OF DENTAL RESEARCH; v. 98, n. 3, p. 347-354, MAR 2019.
Web of Science Citations: 1
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. (AU)

FAPESP's process: 13/05822-9 - Proteinase-Activated Receptors (PARs) in the dentin-pulp complex: identification, modulation and signal tranduction in caries disease
Grantee:Fábio Dupart Nascimento
Support Opportunities: Research Grants - Young Investigators Grants
FAPESP's process: 14/22899-8 - Effect of remineralizing agents on proteolytic activity of caries-affected dentin and on and resin/dentin bond
Grantee:Jossaria Pereira de Sousa
Support Opportunities: Scholarships in Brazil - Doctorate
FAPESP's process: 15/03964-6 - Glycosaminoglycans and proteoglycans: interplay between structure and function
Grantee:Helena Bonciani Nader
Support Opportunities: Research Projects - Thematic Grants
FAPESP's process: 15/12660-0 - Effect of remineralizing agents on proteolytic activity and resin/caries-affected dentin bond longevity
Grantee:Regina Maria Puppin Rontani
Support Opportunities: Regular Research Grants