) 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 P 11 8 in the PCL fibrous structure.

A structurally robust electrospun peptide-enriched scaffold, with controlled peptide release behaviour, supports nucleation and growth of hydroxyapatite minerals in vitro.

Self-assembling peptides (SAPs) have the ability to spontaneously assemble into ordered nanostructures enabling the manufacture of 'designer' nanomaterials. The reversible molecular association of SAPs has been shown to offer great promise in therapeutics via for example, the design of biomimetic assemblies for hard tissue regeneration. This could be further exploited for novel nano/micro diagnostic tools. However, self-assembled peptide gels are often associated with inherent weak and transient mechanical properties. Their incorporation into polymeric matrices has been considered as a potential strategy to enhance their mechanical stability. This study focuses on the incorporation of an 11-residue peptide, P 11 -8 (peptide sequence: CH 3 COGln-Gln-Arg-Phe-Orn-Trp-Orn-Phe-Glu-Gln-Gln-NH 2 ) within a fibrous scaffold of poly ( -caprolactone) (PCL). In this study an electrospinning technique was used to fabricate a biomimetic porous scaffold out of a solution of P 11 -8 and PCL which resulted in a biphasic structure composed of submicron fibers (diameter of 100-700 nm) and nanofibers (diameter of 10-100 nm). The internal morphology of the fabric and its micro-structure can be easily controlled by changing the peptide concentration. The secondary conformation of P 11 -8 was investigated in the as-spun fibers by ATR-FTIR spectroscopy and it is shown that peptide selfassembly into -sheet tapes has taken place during fiber formation and the deposition of the fibrous web.

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