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Self-assembling peptides (SAPs) have the ability to spontaneously assembleinto ordered nanostructures enabling the manufacture of "designer"nanomaterials. The reversible molecular association of SAPs has been shown tooffer great promise in therapeutics via for example, the design of biomimeticassemblies for hard tissue regeneration. This could be further exploited fornovel nano/micro diagnostic tools. However, self-assembled peptide gels areoften associated with inherent weak and transient mechanical properties. Theirincorporation into polymeric matrices has been considered as a potentialstrategy to enhance their mechanical stability. This study focuses on theincorporation of an 11-residue peptide, P11-8 (peptide sequence:CH3CO-Gln-Gln-Arg-Phe-Orn-Trp-Orn-Phe-Glu-Gln-Gln-NH2) within a fibrousscaffold of poly ({\epsilon}-caprolactone) (PCL). In this study anelectrospinning technique was used to fabricate a biomimetic porous scaffoldout of a solution of P11-8 and PCL which resulted in a biphasic structurecomposed of submicron fibers (diameter of 100-700 nm) and nanofibers (diameterof 10-100 nm). The internal morphology of the fabric and its micro-structurecan be easily controlled by changing the peptide concentration. The secondaryconformation of P11-8 was investigated in the as-spun fibers by ATR-FTIRspectroscopy and it is shown that peptide self-assembly into \{b}eta-sheettapes has taken place during fiber formation and the deposition of the fibrousweb.

An investigation into the nano-/micro-architecture of electrospun poly ({\epsilon}-caprolactone) and self-assembling peptide fibers