Front cover in Chemistry—A European Journal

Our recent paper on Acid⋅⋅⋅Amide Supramolecular Synthon for Tuning Amino Acid-Based Hydrogels’ Properties was selected for the front cover of Chemistry—A European Journal.

Read more about the article: Acid⋅⋅⋅Amide Supramolecular Synthon for Tuning Amino Acid-Based Hydrogels’ Properties.
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Acid···Amide Supramolecular Synthon for Tuning Amino Acid-Based Hydrogels’ Properties

Eleonora Veronese, Dr. Claudia Pigliacelli, Dr. Greta Bergamaschi, Prof. Giancarlo Terraneo, Prof. Valentina Dichiarante and Prof. Pierangelo Metrangolo have recently published an article on Chemistry—A European Journal about "Pivotal role of the protein corona in the cell uptake of fluorinated nanoparticles with increased sensitivity for ¹⁹F-MR imaging".

The full paper can be found at the following link: Acid···Amide Supramolecular Synthon for Tuning Amino Acid-Based Hydrogels’ Properties.

Abstract. Supramolecular hydrogels formed by the self-assembly of N-Fmoc-L-phenylalanine derivatives are gaining relevance for several applications in the materials and biomedical fields. In the challenging attempt to predict or tune their properties, we selected Fmoc-pentafluorophenylalanine (1) as a model efficient gelator, and studied its self-assembly in the presence of benzamide (2), a non-gelator able to form strong hydrogen bonding with the amino acid carboxylic group. Equimolar mixtures of 1 and 2 in organic solvents afforded a 1:1 co-crystal thanks to the formation of an acid···amide heterodimeric supramolecular synthon. The same synthon occurred in the transparent gels formed by mixing the two components in 1:1 ratio in aqueous media, as revealed by structural, spectroscopic, and thermal characterizations performed on both the co-crystal powder and the lyophilized hydrogel. These findings revealed the possibility to modulate the properties of amino acid-based hydrogels, by involving the gelator in the formation of a co-crystal. Such crystal engineering-based approach is demonstrated to be also useful for the time-delayed release of suitable bioactive molecules, when involved as hydrogel coformers.

How to cite:
Eleonora Veronese, Claudia Pigliacelli, Greta Bergamaschi, Giancarlo Terraneo, Valentina Dichiarante and Pierangelo Metrangolo Acid···Amide Supramolecular Synthon for Tuning Amino Acid-Based Hydrogels’ Properties, Chem. Eur. J., 2023, e202301743.
DOI: https://doi.org/10.1002/chem.202301743

Computation meets experiment: identification of highly efficient fibrillating peptides

Lorenzo Sori, Andrea Pizzi, Pierangelo Metrangolo, and others have recently published an article on CrystEngComm about "Computation meets experiment: identification of highly efficient fibrillating peptides".

The full paper can be found at the following link: Computation meets experiment: identification of highly efficient fibrillating peptides.

Abstract. Self-assembling peptides are of huge interest for biological, medical and nanotechnological applications. The enormous chemical variety that is available from the 20 amino acids offers potentially unlimited peptide sequences, but it is currently an issue to predict their supramolecular behavior in a reliable and cheap way. Herein we report a computational method to screen and forecast the aqueous self-assembly propensity of amyloidogenic pentapeptides. This method was found also as an interesting tool to predict peptide crystallinity, which may be of interest for the development of peptide based drugs.

How to cite:
Lorenzo Sori, Andrea Pizzi, Greta Bergamaschi, Alessandro Gori, Alfonso Gautieri, Nicola Demitri, Monica Soncini and Pierangelo Metrangolo, Computation meets experiment: identification of highly efficient fibrillating peptides, CrystEngComm , 2023, TBD
DOI: https://doi.org/10.1039/D3CE00495C

Pivotal role of the protein corona in the cell uptake of fluorinated nanoparticles with increased sensitivity for ¹⁹F-MR imaging

Lodovico Gatti, Dr. Cristina Chirizzi, Pietro Milesi, Prof. Pierangelo Metrangolo, Prof. Francesca Baldelli Bombelli and others have recently published an article on Nanoscale Advances about "Pivotal role of the protein corona in the cell uptake of fluorinated nanoparticles with increased sensitivity for ¹⁹F-MR imaging".

The full paper can be found at the following link: Pivotal role of the protein corona in the cell uptake of fluorinated nanoparticles with increased sensitivity for ¹⁹F-MR imaging.

Abstract. In vivo cell tracking by non-invasive imaging technologies is needed to accelerate the clinical translation of innovative cell-based therapies. In this regard, ¹⁹F-MRI has recently gained increased attention for unbiased localization of labeled cells over time. To push forward the use of ¹⁹F-MRI for cell tracking, the development of highly performant ¹⁹F-probes is required. PLGA-based NPs containing PERFECTA, a multibranched superfluorinated molecule with an optimal MRI profile thanks to its 36 magnetically equivalent fluorine atoms, are promising ¹⁹F-MRI probes. In this work we demonstrate the importance of the surface functionalization of these NPs in relation to their interaction with the biological environment, stressing the pivotal role of the formation of the protein corona (PC) in their cellular labelling efficacy. In particular, our studies showed that the formation of PC NPs strongly promotes the cellular internalization of these NPs in microglia cells. We advocate that the formation of PC NPs in the culture medium can be a key element to be used for the optimization of cell labelling with a considerable increase of the detection sensitivity by 19F-MRI.

How to cite:
Lodovico Gatti, Cristina Chirizzi, Giulia Rotta, Pietro Milesi, María Sancho-Albero, Victor Sebastián, Anna Mondino, Jesús Santamaría, Pierangelo Metrangolo, Linda Chaabane and Francesca Baldelli Bombelli Pivotal role of the protein corona in the cell uptake of fluorinated nanoparticles with increased sensitivity for ¹⁹F-MR imaging, Nanoscale Adv., 2023, 5, 3749-3760
DOI: https://doi.org/10.1039/D3NA00229B