Ricerc@Sapienza

Enzyme immobilization on nanocarriers is nowadays considered a useful tool for improving activity and maintaining biocatalysts stability while facilitating their recovery and reuse. In this work we prepared Au and Ag based nanoparticles (AuNPs or AgNPs) stabilized with two different ligands, the organometallic dinuclear complex trans,trans-[dithiodibis(tributylphosphine)diplatinum(II)-4,4'-diethynylbiphenyl] (Pt-DEBP) and the organic dithiol 4,4'-dithiol-biphenyl (BI), able to link the NPs in 3D networks.

Lipase-immobilized nanomaterials with high activity and stable reusability would have a great impact in different fields. However, developing such materials has proven to be challenging. Herein, polymer (pAcDED)-coated magnetic nanoparticles (MNPs) displaying long alkyl chains, either octyl (C8) or hexadecyl (C16), have been prepared and used for immobilization of Candida rugosa lipase. The aim of the study was to develop magnetic supports able to bind enzyme via interfacial activation thus to stabilized the lipase open conformation.

Peptide-based hydrogels have been widely used for both tissue engineering approaches and therapeutic drug delivery mainly thanks to their tissue-like water content and tunable physicochemical properties. In particular, the modulation of the hydrogel chemical structure influences hydrogel properties. The most common approach for tuning hydrogel properties in terms of cell adhesion or release efficiency of entrapped compounds is chemical crosslinking.

A newly modified electrode based on glassy carbon (GC) has been prepared and characterized electrochemically for application in electroanalytical chemistry. In particular, a GC screen-printed electrode (SPE) has been modified with nanostructures, namely multi-walled carbon nanotubes (MWCNTs), and TiO2 nanoparticles, and combined with a new generation of eco-friendly room-temperature ionic liquids (RTILs).

The applications of peptide-based materials are currently expanding, especially in the biomedical field. The biocompatibility and biodegradability of peptide materials, as well as their ability to assemble into ordered secondary structures, are indeed ideal for biotechnological applications. However, their full potential will be exploited once novel synthetic procedures are developed for advanced applications. In this work, we explored the ability of Pseudomonas fluorescens lipase to biosynthesize the self-assembled tetrapeptide FmocPheGlyPhe2 for tissue regeneration.