Peptide-based scaffolds are a frontier research area in materials science with widespread impact in biomedical engineering. In this paper, we describe a hybrid material formulated through the conjugation of electrospun polycaprolactone (PCL) fibers and micro/nanotubes of L,L-diphenylalanine (FF-MNTs). Morphology and crystallinity of the composite matrices are investigated using a wide range of analytical techniques including electron microscopy, thermal analyses, X-ray diffraction and micro-tomography. Peptide assemblies are found to produce deep modifications on the microstructure of PCL fibers, impacting average diameters, crystallinity degree and porous size in the polymer network. These changes are correlated with mechanical properties of the resulting scaffolds, whose strength is found to exhibit a brittle-to-ductile transition upon increasing the amount of FF-MNTs and lead to enhanced Young's moduli of polymer fibers. The PCL/FF-MNTs composites were tested for the drug delivery application of a lipophilic drug, benzocaine. In vitro permeation studies have shown that these polymer/peptide hybrids are able to produce a steady release of benzocaine over periods of up to ∼13 hours, much higher than commercially available gel formulations. Enzymatic tests have shown a significant increment in biodegradation rates in PCL/FF-MNTs hybrids containing higher peptide amounts, which exhibited almost 100% weight loss against only 10% found in pure PCL. Our findings indicate that using PCL/FF-MNTs materials is a simple route towards achieving enhanced mechanical strength of PCL networks that have the ability to promote controlled drug delivery from a completely biodegradable matrix.

A novel enzymatic platform for the sensing of H₂O₂ and glucose that uses L,L-diphenylalanine micro/nanostructures (FF-MNSs) as an enzyme support is shown. This platform is obtained by the self-assembly of poly(allylamine hydrochloride) (PAH), FF-MNSs, and microperoxidase-11 (MP11) anchored onto the peptide matrix, in two different crystal structures of FF-MNSs: hexagonal (P6₁) and orthorhombic (P22₁2₁). The electroactive area of the electrodes increases in the presence of FF-MNSs. We also demonstrate via theoretical calculations that the valence band energy of the orthorhombic structure allows it to be doped, similarly to p-type semiconductors, where PAH acts as a doping agent for the orthorhombic peptide structure, decreasing the band-gap by around 1 eV, which results in a smaller charge transfer resistance. These results are consistent with electrochemical impedance spectroscopy measurements, which further elucidate the role of the band structure of the orthorhombic FF-MNSs in the conductivity and electron transfer rates of the hybrid material. An effective communication between the electrode and the active site of a glucose oxidase enzyme through MP11–protein complexes occurs, paving the way for FF-MNSs in the orthorhombic phase for the future development of bioelectronics sensing devices.