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,
P11-8 (peptide sequence:
within a fibrous scaffold of poly (ε-caprolactone) (PCL). In this
study an electrospinning technique was used to fabricate a biomimetic porous
scaffold out of a solution of P11-8 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 P11-8 was investigated
in the as-spun fibers by ATR-FTIR spectroscopy and it is shown that peptide
self-assembly into β-sheet tapes has taken place during fiber
formation and the deposition of the fibrous web.