跳至主要内容

Acquired Enamel Pellicle Engineered Peptides: Effects on Hydroxyapatite Crystal Growth

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
标签：

评论

发表评论

此博客中的热门博文

The Catalytically Inactive Mutation of the Ubiquitin-Conjugating Enzyme CDC34 Affects its Stability and Cell Proliferation

Author：Xun Liu, Yang Zhang, Zhanhong Hu, Qian Li, Lu Yang,  Guoqiang Xu     《The Protein Journal》 ABSTRACTS The ubiquitin proteasome system (UPS) plays important roles in the regulation of protein stability, localization, and activity. A myriad of studies have focused on the functions of ubiquitin ligases E3s and deubiquitinating enzymes DUBs due to their specificity in the recognition of downstream substrates. However, the roles of the most ubiquitin-conjugating enzymes E2s are not completely understood except that they transport the activated ubiquitin and form E2–E3 protein complexes. Ubiquitin-conjugating enzyme CDC34 can promote the degradation of downstream targets through the UPS whereas its non-catalytic functions are still elusive. Here, we find that mutation of the catalytically active cysteine to serine (C93S) results in the reduced ubiquitination, increased stability, and attenuated degradation rate of CDC34. Through semi-quantitative proteom...
发表评论
阅读全文

Identification and Inhibitory Mechanism of Angiotensin I-Converting Enzyme Inhibitory Peptides Derived from Bovine Hemoglobin

Author：Ying Wang, Yiqun Jiang, Yongguang Yin, Jiyun Liu,  Long Ding, Jingbo Liu, Ting Zhang     《The Protein Journal》 ABSTRACTS Angiotensin I-converting enzyme (ACE, EC.3.4.15.1) inhibitory peptide is an efficacious therapy for hypertension. In this study, four dipeptides, TY, FD, FL and FG, were identified from the desalted fraction of bovine hemoglobin hydrolysate, obtained by in vitro simulated gastrointestinal digestion, via liquid chromatography-tandem mass spectrometry (LC-MS/MS). The IC 50   value of TY and FL are 96.43?±?6.17 and 290.66?±?57.92  μM, respectively. The result of molecular docking indicated that TY occupied the ACE subsite S1 and S1′ with a lowest estimated binding energy of ?9.96  Kcal/mol, while FL occupied the subsite S5 with a lowest estimated binding energy of ?9.37  Kcal/mol. The subsite S1′ and S2′ are closer to the ACE active center (Zn 2+ ) than S5, and the lowest estimated binding energy of TY is lower ...
发表评论
阅读全文

Preparation of an antimicrobial surface by direct assembly of antimicrobial peptide with its surface binding activity

Author：Junjian Chen, Yuchen Zhu, Yancheng Song, Lin Wang,  Jiezhao Zhan, Jingcai He, Jian Zheng, Chunting Zhong, Xuetao Shi, Sa Liu, Li Ren and Yingjun Wang     《Journal of Materials Chemistry B》 ABSTRACTS Antimicrobial peptides (AMPs) are a broad prospect for clinical application against bacterial infections of biomaterials. However, a bottleneck exists as there is a lack of simple technology to prepare AMPs on biomaterials with sufficient activity, as the activity of AMP is dependent on the correct orientation on the biomaterial. In the present study, based on the conventional AMP (Tet213: KRWWKWWRRC) and surface binding peptide (SKHKGGKHKGGKHKG), we designed an Anchor-AMP that could be directly assembled onto the surface of the biomaterial and also showed excellent antimicrobial activity. By characterizing the surface using a quartz crystal microbalance with dissipation (QCM-D), contact angle, atom force microscopy (AFM) and X-ray photoelectron spectr...
发表评论
阅读全文