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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

Effect of dental tissue conditioners and matrix metalloproteinase inhibitors on type I collagen microstructure analyzed by Fourier transform infrared spectroscopy

Texto completo
Autor(es):
Botta, Sergio B. [1] ; Ana, Patricia A. [2] ; Santos, Moises O. [3] ; Zezell, Denise M. [3] ; Matos, Adriana B. [1]
Número total de Autores: 5
Afiliação do(s) autor(es):
[1] Univ Sao Paulo, Sch Dent, Dept Operat Dent, Sao Paulo - Brazil
[2] Fed Univ ABC, Biomed Engn Ctr Engn Modeling & Appl Social Sci, Santo Andre, SP - Brazil
[3] Ctr Lasers & Applicat, Energet & Nucl Res Inst, Sao Paulo - Brazil
Número total de Afiliações: 3
Tipo de documento: Artigo Científico
Fonte: JOURNAL OF BIOMEDICAL MATERIALS RESEARCH PART B-APPLIED BIOMATERIALS; v. 100B, n. 4, p. 1009-1016, MAY 2012.
Citações Web of Science: 19
Resumo

This study aimed to evaluate the chemical interaction of collagen with some substances usually applied in dental treatments to increase the durability of adhesive restorations to dentin. Initially, the similarity between human dentin collagen and type I collagen obtained from commercial bovine membranes of Achilles deep tendon was compared by the Attenuated Total Reflectance technique of Fourier Transform Infrared (ATR-FTIR) spectroscopy. Finally, the effects of application of 35% phosphoric acid, 0.1M ethylenediaminetetraacetic acid (EDTA), 2% chlorhexidine, and 6.5% proanthocyanidin solution on microstructure of collagen and in the integrity of its triple helix were also evaluated by ATR-FTIR. It was observed that the commercial type I collagen can be used as an efficient substitute for demineralized human dentin in studies that use spectroscopy analysis. The 35% phosphoric acid significantly altered the organic content of amides, proline and hydroxyproline of type I collagen. The surface treatment with 0.1M EDTA, 2% chlorhexidine, or 6.5% proanthocyanidin did not promote deleterious structural changes to the collagen triple helix. The application of 6.5% proanthocyanidin on collagen promoted hydrogen bond formation. (c) 2012 Wiley Periodicals, Inc. J Biomed Mater Res Part B: Appl Biomater, 2012. (AU)

Processo FAPESP: 06/06746-0 - Consolidação de metodologia para avaliação dos efeitos da irradiação laser na prevenção da cárie radicular
Beneficiário:Patricia Aparecida da Ana
Linha de fomento: Bolsas no Brasil - Pós-Doutorado
Processo FAPESP: 06/05684-1 - A contaminação com saliva influencia na adesão aos tecidos dentais?
Beneficiário:Adriana Bona Matos
Linha de fomento: Auxílio à Pesquisa - Regular
Processo FAPESP: 05/51689-2 - Centro de Pesquisa em Óptica e Fotônica - UNICAMP (CEPOF-UNICAMP)
Beneficiário:Hugo Luis Fragnito
Linha de fomento: Auxílio à Pesquisa - Centros de Pesquisa, Inovação e Difusão - CEPIDs