Abstract
The rise of drug-resistant microorganisms has prompted the development of innovative strategies with the aim of addressing this challenge. Among the alternative approaches gaining increased attention are antimicrobial peptides (AMPs), a group of peptides with the ability to combat microbial pathogens. Here, we investigated a small peptide, KLVFF, derived from the Alzheimer's amyloid-β (Aβ) protein. While Aβ has been associated with the development of neurodegenerative diseases, the core part of the Aβ protein, namely the Aβ 16-20 fragment, has also been exploited to obtain highly functional biomaterials. In this study we found that KLVFF is capable of self-assembling into a fibrillar network to form a self-healing hydrogel. Moreover, this small peptide can undergo a transition from a gel to a liquid state following application of shear stress, in a reversible manner. As an AMP, this material exhibited both antibacterial and antifungal properties while remaining highly biocompatible and noncytotoxic toward mammalian cells. The propensity of the KLVFF hydrogel to rapidly assemble into highly ordered macroscopic structures makes it an ideal candidate for biomedical applications necessitating antimicrobial activity, such as wound healing.