Published online by Cambridge University Press: 20 January 2016
Self-assembling peptides (SAPs) have the ability to spontaneously assemble intoordered nanostructures enabling the manufacture of‘designer’ nanomaterials. The reversible molecularassociation of SAPs has been shown to offer great promise in therapeutics viafor 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 andtransient mechanical properties. Their incorporation into polymeric matrices hasbeen considered as a potential strategy to enhance their mechanical stability.This study focuses on the incorporation of an 11-residue peptide,P11-8 (peptide sequence:CH3CO-Gln-Gln-Arg-Phe-Orn-Trp-Orn-Phe-Glu-Gln-Gln-NH2)within a fibrous scaffold of poly (ε-caprolactone) (PCL). In thisstudy an electrospinning technique was used to fabricate a biomimetic porousscaffold out of a solution of P11-8 and PCL which resulted in abiphasic structure composed of submicron fibers (diameter of 100-700 nm) andnanofibers (diameter of 10-100 nm). The internal morphology of the fabric andits micro-structure can be easily controlled by changing the peptideconcentration. The secondary conformation of P11-8 was investigatedin the as-spun fibers by ATR-FTIR spectroscopy and it is shown that peptideself-assembly into β-sheet tapes has taken place during fiberformation and the deposition of the fibrous web.