Enhancing bond strength on demineralized dentin by pre-treatment with selective remineralising agents.

Bonding to demineralized dentin of a diseased tooth has shown to be a significant clinical issue. This study evaluated the effect of 0.2% NaF-(NaF), MI Paste™-(CPP-ACP) and the self-assembling peptide 'P11-4' (Ace-QQRFEWEFEQQ-NH2) contained in Curodont™ Repair, have on microtensile bond strength-(µTBS) of two different adhesive systems (Adper™ Single Bond-(SB) or Clearfil™ SE Bond (CSE)) and wettability of demineralized dentin slices after remineralising agents were applied. The highest µTBS were found for the demineralized dentin-(DD) treated with CPP-ACP; both adhesives systems (p < 0.05) did not significantly difference from P11-4 treatment associated with SB, and also presented higher values than sound dentin-(SD/SB) (p < 0.01). DD treated with P11-4 associated with CSE did not differ from DD/CSE (p > 0.05). The NaF treatment associated with CSE recovered the bond strength values of SD/CSE and associated with CSE demonstrated lower µTBS than other groups, although significantly higher than DD (p < 0.05). P11-4 and CPP-ACP increased significantly the wettability of demineralized dentin (p < 0.05); etching acid improved wettability for all groups (p < 0.05), whilst NaF did not affect the wettability of demineralized dentin (p > 0.05). Morphological analysis of the dentin surface and dentin-resin interface revealed unique features of the applied remineralizing agent. The results indicated that self-assembling peptide P11-4 associated with SB and CPP-ACP associated with SB or CSE significantly enhanced the bond strength to demineralized dentin (p < 0.05). We conclude that by modifying the dentine surface and restoring conditions found on sound dentin, this can enhance the interfacial bonding.

Peptide strand length controls the energetics of self-assembly and morphology of ß-sheet fibrils.

Self-assembling peptides can be used as versatile, natural, and multifunctional building blocks to produce a variety of well-defined nanostructures, materials and devices for applications in medicine and nanotechnology. Here, we concentrate on the 1D self-assembly of de novo designed Px-2 peptide ß-strands into anti-parallel ß-sheet tapes and higher order aggregates. We study six members of the Px-2 family, ranging from 3 amino acids (aa) to 13 aa in length, using a range of complementary experimental techniques, computer simulation and theoretical statistical mechanics. The critical concentration for self-assembly (c*) is found to increase systematically with decreasing peptide length. The shortest peptide found to self-assemble into soluble ß-tapes in water is a 5 amino acid residue peptide. These investigations help decipher the role of the peptide length in controlling self-assembly, aggregate morphology, and material properties. By extracting free energies from these data using a statistical mechanical analysis and combining the results with computer simulations at the atomistic level, we can extract the entropy of association for individual ß-strands.

Poly(amino acid)-polyester graft copolymer nanoparticles for the acid-mediated release of doxorubicin.

Biodegradable polymers have emerged as highly effective drug delivery vehicles. We combine N-carboxyanhydride and O-carboxyanhydride ring opening polymerisations to synthesise a poly(amino acid)-polyester graft copolymer capable of encapsulating, and subsequently releasing doxorubicin via acid-mediated hydrolysis. Consequently, the nanoparticles detailed are extremely promising vehicles for the controlled delivery of chemotherapeutic agents.

A structurally self-assembled peptide nano-architecture by one-step electrospinning.

Self-assembling peptides (SAPs) have been shown to offer great promise in therapeutics and have the ability to undergo self-assembly and form ordered nanostructures. However SAP gels are often associated with inherent weak and transient mechanical properties and incorporation of them into polymeric matrices is a route to enhance their mechanical stability. The aim of this work was to incorporate P11-8 peptide (CH3COQQRFOWOFEQQNH2) within poly(ε-caprolactone) (PCL) fibrous webs via one-step electrospinning, aiming to establish the underlying relationships between spinning process, molecular peptide conformation, and material internal architecture. Electrospinning of PCL solutions (6% w/w) in hexafluoro-2-propanol (HFIP) containing up to 40 mg mL-1 P11-8 resulted in the formation of fibres in both nano- (10-100 nm) and submicron range (100-700 nm), in contrast to PCL only webs, which displayed a predominantly submicron fibre distribution. FTIR and CD spectroscopy on both PCL/peptide solutions and resulting electrospun webs revealed monomeric and ß-sheet secondary conformation, respectively, suggesting the occurrence of peptide self-assembly during electrospinning due to solvent evaporation. The peptide concentration (0 → 40 mg mL-1) was found to primarily affect the internal structure of the fabric at the nano-scale, whilst water as well as cell culture medium contact angles were dramatically decreased. Nearly no cytotoxic response (>90% cell viability) was observed when L929 mouse fibroblasts were cultured in contact with electrospun peptide loaded samples. This novel nanofibrous architecture may be the basis for an interesting material platform for e.g. hard tissue repair, in light of the presence of the self-assembled P11-8 in the PCL fibrous structure.