Self-assembly peptide P-4 induces mineralization and cell-migration of odontoblast-like cells.

Objectives: Self-assembling peptide P-4 is amphiphilic and pH-triggered, effective on repairing early enamel carious lesions and dentin remineralization. However, P-4 effects on dentin biomineralization and repair ability remain unexplored. Thus, cytocompatibility and effectiveness of P-4 on inducing mineralization and migration of odontoblast-like cells (MDPC-23) were investigated.

An Intraoral Defect Model for Assessing the Use of P-4 Self-Assembling Peptide in Periodontal Regeneration.

Periodontal disease is one of the most common diseases worldwide. It has a significant impact on oral health and subsequently the individual's quality of life. However, optimal regeneration of periodontal tissues, using current treatments, has yet to be achieved.

Biomimetic Mineralizing Agents Recover the Micro Tensile Bond Strength of Demineralized Dentin.

Biomimetic remineralization is an approach that mimics natural biomineralization, and improves adhesive procedures. The aim of this paper was to investigate the influence of Dentin Caries-like Lesions (DCLL)-Producing Model on microtensile bond strength (μTBS) of etch and rinse adhesive systems and investigate the effect of remineralizing agents such as Sodium Fluoride (NaF), MI Paste™ (MP) and Curodont™ Repair (CR) on caries-affected dentin (n = 6). Nine groups were established: (1) Sound dentin; (2) Demineralized dentin/Chemical DCLL: (3) Demineralized dentin/Biological DCLL; (4) Chemical/DCLL + NaF; (5) Chemical/DCLL + MP; (6) Chemical/DCLL + CR; (7) Biological/DCLL + NaF; (8) Biological/DCLL + MP; (9) Biological/DCLL + CR.

Self-assembly of amphiphilic β-sheet peptide tapes based on aliphatic side chains.

Amphiphilic β-sheet nanotapes based on the self-assembly of 9mer and 7mer de novo designed β-strand peptides were studied in the dilute regime. The hydrophobic face of the tapes consisted predominantly of aliphatic (leucine) side chains, while the hydrophilic tape face contained polar side chains (glutamine, arginine and glutamic acid). Both peptides underwent a transition from a monomeric random coil to a self-assembled β-sheet tape upon increase of peptide concentration in aqueous solutions.