Water-Soluble Star Polymer as a Potential Photoactivated Nanotool for Lysozyme Degradation

Author:

Mezzina Lidia1ORCID,Nicosia Angelo1ORCID,Barone Laura1,Vento Fabiana1ORCID,Mineo Placido Giuseppe123ORCID

Affiliation:

1. Department of Chemical Sciences and INSTM UdR of Catania, University of Catania, V.le A. Doria 6, I-95125 Catania, Italy

2. Institute for Chemical and Physical Processes, National Research Council (IPCF-CNR), Viale F. Stagno d’Alcontres 37, I-98158 Messina, Italy

3. Institute of Polymers, Composites and Biomaterials, National Research Council (IPCB-CNR), Via P. Gaifami 18, I-95126 Catania, Italy

Abstract

The development of nanotools for chemical sensing and macromolecular modifications is a new challenge in the biomedical field, with emphasis on artificial peptidases designed to cleave peptide bonds at specific sites. In this landscape, metal porphyrins are attractive due to their ability to form stable complexes with amino acids and to generate reactive oxygen species when irradiated by light of appropriate wavelengths. The issues of hydrophobic behavior and aggregation in aqueous environments of porphyrins can be solved by using its PEGylated derivatives. This work proposes the design of an artificial photo-protease agent based on a PEGylated mercury porphyrin, able to form a stable complex with l-Tryptophan, an amino acid present also in the lysozyme structure (a well-known protein model). The sensing and photodegradation features of PEGylated mercury porphyrin were exploited to detect and degrade both l-Trp and lysozyme using ROS, generated under green (532 nm) and red (650 nm) light lasers. The obtained system (Star3600_Hg) and its behavior as a photo-protease agent were studied by means of several spectroscopies (UV-Vis, fluorescence and circular dichroism), and MALDI-TOF mass spectrometry, showing the cleavage of lysozyme and the appearance of several short-chain residues. The approach of this study paves the way for potential applications in theranostics and targeted bio-medical therapies.

Funder

European Union

Publisher

MDPI AG

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