文献作者：Maria Teresa Valente, Eduardo Buozi Moffa, Karla Tonelli Bicalho Crosara, Yizhi Xiao, Thais Marchini de Oliveira, Maria Aparecida de Andrade Moreira Machado & Walter Luiz Siqueira 《SCIENTIFIC REPORTS》
ABSTRACTS
The aim of this study was to test the hypothesis that duplication/hybridization of functional domains of naturally occurring pellicle peptides amplified the inhibitory effect of hydroxyapatite crystal growth, which is related to enamel remineralization and dental calculus formation. Histatin 3, statherin, their functional domains (RR14 and DR9), and engineered peptides (DR9-DR9 and DR9-RR14) were tested at seven different concentrations to evaluate the effect on hydroxyapatite crystal growth inhibition. A microplate colorimetric assay was used to quantify hydroxyapatite crystal growth. The half-maximal inhibitory concentration (IC50) was determined for each group. ANOVA and Student-Newman-Keuls pairwise comparisons were used to compare the groups. DR9-DR9 increased the inhibitory effect of hydroxyapatite crystal growth compared to single DR9 , indicating that functional domain multiplication represented a strong protein evolution pathway. Interestingly, the hybrid peptide DR9-RR14 had an intermediate inhibitory effect compared to DR9 and DR9-DR9. This study used an engineered peptide approach to investigate a potential evolution protein pathway related to duplication/hybridization of acquired enamel pellicle’s natural peptide constituents, contributing to the development of synthetic peptides for therapeutic use against dental caries and periodontal disease.
SCREENSHOT
RELATED PRODUCTS
Engineered novel peptides derived from the functional domains of statherin and histatin 3—DR9, RR14, DR9-DR9, and DR9-RR14 were chemically synthesized by Chinapeptide (Shanghai, China)
CHAINING
https://www.nature.com/articles/s41598-018-21854-4
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