Andrea Lapini received the master degree in Chemistry in 2005 from the University of Florence (110/110) and the PhD In Chemical Science from the Science Doctorate School of the University of Florence and the European Laboratory for Non-Linear Spectroscopy (LENS). During the PhD he developed a pronounced interest towards the usage of Coherent Ultrafast Spectroscopy to disentangle electronic and structural properties of simple and complex molecular systems. He spent the years between 2009 and 2017 as a pots-doctoral fellow @ LENS developing most of instrumentation nowadays employed to performed 2DIR and 2D-Visible spectroscopy. In 2018 Andrea got a permanent position as a researcher in the National Institute of Metrological Research (INRIM) in Turin, within the Advanced Material and Life Science division. In 2021 Andrea got a position as a Tenure-track Assistant Professor in Physical Chemistry at the Department of Chemistry, Life Science and Environmental Sustainability in Parma.
EDUCATION
Andrea Lapini received the master degree in Chemistry in 2005 from the University of Florence (110/110) and the PhD In Chemical Science from the Science Doctorate School of the University of Florence and the European Laboratory for Non-Linear Spectroscopy (LENS).
RESEARCH INTERESTS
Ultrafast Spectroscopy, Non Linear Microscopy, Non Linear Optics, regenerative medicine.
59
Scopus Publications
Scopus Publications
Geometry Controls Confined Water Dynamics in Lipidic Mesophases Sara Catalini, Matteo Rutsch, Andrea Lapini, Barbara Rossi, Mariangela Di Donato, Brenda Bracco, Marco Paolantoni, Yang Yao Angewandte Chemie International Edition, 2026 Water under nanoscale confinement is central to biological function, catalysis, and soft materials, yet how geometry dictates its structure and dynamics remains unresolved. Here, we establish a direct link between interfacial curvature and confined water behavior using an archaeal‐inspired phytantriol‐water lipidic mesophase platform. By systematically tuning curvature across lamellar, double‐gyroid cubic, and reverse micellar phases, and integrating structural, thermodynamic, and ultrafast spectroscopies, we show that geometry controls the dimensionality and mobility of the hydrogen‐bond network. Planar interfaces enforce 2D networks that slow down interfacial water through spatial constrain, whereas curved bicontinuous and micellar topologies promote 3D networks with accelerated reorientation. These findings reveal a geometric principle for governing water dynamics in soft nanoconfinement, providing molecular level design rules for confined transport and reactivity in membranes and functional materials.
Supramolecular topological adhesion boosts delamination resistance in carbon fiber reinforced polymers Monica Milani, Silvia D’Auria, Francesco Bertocchi, Alice Boschetti, Andrea Lapini, Alberto Fina, Alessandro Pedrini, Roberta Pinalli, Chiara Pernechele, Enrico Dalcanale Advanced Composites and Hybrid Materials, 2026 In this study, we introduce supramolecular topological adhesion as an innovative and effective methodology to enhance interlaminar fracture toughness in carbon fiber reinforced polymers (CFRPs). We achieved remarkable improvements in delamination resistance by physically entangling phenoxy resins within an epoxy matrix and introducing sacrificial H-bond interactions via ODIN (1-(7-Oxo-7,8-Dihydro-1,8-Naphthyridin-2-yl)urea) units. The ODIN units form sextuple H-bonding dimers in the cured epoxy matrix among plies, experimentally quantified via UV–Vis spectroscopy, whose detachment hinders crack propagation. The viability of this approach was tested using various phenoxy resins with different molecular weights and with different levels of ODIN functionalization. Single lap shear (SLS) tests demonstrated a notable increase in adhesion strength, pointing out PKHB-ODIN 13% as the best candidate as interlaminar adherent. Delamination resistance was determined through double cantilever beam (DCB) and end-notched flexure (ENF) tests, showing up to 120% and 80% increases in Mode I and Mode II fracture toughness, respectively. The limited DCB and ENF test increments observed for control adherent PKHB-PU 23% functionalized with phenylurea (PU) groups, demonstrates that the strength of topological H-bonding is pivotal to boost delamination resistance. The results indicate that this method holds great potential for improving the durability of CFRP composites, especially in applications requiring high resistance to delamination.
Self-assembly of boc-protected diphenylalanine functionalized with boron-dipyrromethane Sara Catalini, Francesca Mancusi, Stefano Cicchi, Mariangela Di Donato, Alessandro Iagatti, Andrea Lapini, Paolo Foggi, Caterina Petrillo, Alessandro Di Michele, Marco Paolantoni, Lucia Comez, Alessandro Paciaroni Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy, 2025 Peptides functionalized with fluorescent dyes can form aggregated structures that show potential for photonic and/or theranostic applications. In this study, we used the good-bad solvent method to induce the self-assembly of chromopeptides into various products, which were characterized using a multi-technique spectroscopic approach. Two hydrophobic chromopeptides were designed by attaching boron-dipyrromethane dyes to Boc-protected diphenylalanine, resulting in spherical aggregates with tunable dimensions, influenced by the compound's molar concentration and solvent composition. These aggregates exhibit distinct optical properties, including bathochromic shifts in absorption and emission bands, as well as induced chirality, suggesting different chromophore orientations within the microspheres. Moreover, the aggregates show accelerated excited-state relaxation compared to monomeric chromopeptides, primarily through non-radiative processes. This work establishes a foundation for future studies focused on optimizing the desired photophysical properties of similar chromopeptide aggregates, depending on their intended application.
Amyloid aggregation in mixed whey proteins Sara Venturi, Barbara Rossi, Fatima Matroodi, Renato Torre, Andrea Lapini, Paolo Foggi, Alessandro Di Michele, Paola Sassi, Marco Paolantoni, Sara Catalini Food Hydrocolloids, 2025 The fundamental principles behind the complexity of protein assembly, especially in mixed protein systems and crowded environments, remain elusive. This study provides molecular, structural, and viscoelastic insights into the aggregation and gelation processes in aqueous solutions of pure and mixed β-lactoglobulin and albumin whey proteins. To better understand protein aggregation in complex systems, we used a multi-technique approach that spans from molecular to macroscopic length scales. Our results show that, under low pH and heat denaturation, β-lactoglobulin tends to form ordered amyloid-type aggregates, while bovine serum albumin forms non-amyloid aggregates. In crowded environments, all protein solutions tested develop composite gel networks with distinct molecular origins. Here the ability to control the amyloid aggregate content, which has a substantial effect on the structural and viscoelastic properties of these composite gels, has been demonstrated. Gel structure and viscosity are crucial parameters to control for the food industry, as they play a key role in determining the softness and texture of food products. • Proteins behave independently of each other but form transparent composite gels. • Gels with higher amyloid content have higher viscosity. • Composite gels have tunable structural and viscoelastic properties.
How the nitro group position determines the emission properties of π-expanded diketopyrrolopyrroles Kamil Skonieczny, Francesco Di Maiolo, Sara Venturi, Alessandro Iagatti, Alessandro Ricci, Francesco Bertocchi, Daniel T. Gryko, Andrea Lapini Physical Chemistry Chemical Physics, 2025 When the nitro group is located at a distant position with respect to the lactam moiety, the expanded DPP exhibits strong emission with optical brightness exceeding 110 000 (M−1 cm−1) in non-polar solvents.
Nanothermometer Based on Polychlorinated Trityl Radicals Showing Two-Photon Excitation and Emission in the Biological Transparency Window: Temperature Monitoring of Biological Tissues Nerea Gonzalez‐Pato, Davide Blasi, Domna M. Nikolaidou, Francesco Bertocchi, Jesús Cerdá, Francesca Terenziani, Nora Ventosa, Juan Aragó, Andrea Lapini, Jaume Veciana, Imma Ratera Small Methods, 2024 Nanothermometers are emerging probes as biomedical diagnostic tools. Especially appealing are nanoprobes using NIR light in the range of biological transparency window (BTW) since they have the advantages of a deeper penetration into biological tissues, better contrast, reduced phototoxicity and photobleaching. This article reports the preparation and characterization of organic nanoparticles (ONPs) doped with two polychlorinated trityl radicals (TTM and PTM), as well as studies of their electronic and optical properties. Such ONPs having inside isolated radical molecules and dimeric excimers, can be two‐photon excited showing optimal properties for temperature sensing. Remarkably, in TTM‐based ONPs the emission intensity of the isolated radical species is unaltered increasing temperature, while the excimer emission intensity decreases strongly being thereby able to monitor temperature changes with an excellent thermal absolute sensitivity of 0.6–3.7% K−1 in the temperature range of 278–328 K. The temperature dependence of the excimeric bands of ONPs are theoretically simulated by using electronic structure calculations and a vibronic Hamiltonian model. Finally, TTM‐doped ONPs as ratiometric NIR‐nanothermometers are tested with two‐photon excitationwith enucleated pig eye sclera, as a real tissue model, obtaining a similar temperature sensitivity as in aqueous suspensions, demonstrating their potential as NIR nanothermometers for bio applications.
Multiple length-scale control of Boc-protected diphenylalanine aggregates through solvent composition Sara Catalini, Francesco Bagni, Stefano Cicchi, Mariangela Di Donato, Alessandro Iagatti, Andrea Lapini, Paolo Foggi, Caterina Petrillo, Alessandro Di Michele, Marco Paolantoni, Giorgio Schirò, Lucia Comez, Alessandro Paciaroni Materials Advances, 2024 Self-aggregation of Boc-protected diphenylalanine towards the formation of architectures with morphology and structure highly dependent on the acetonitrile-water percentage.
Tuning the Optical Properties Through Hydrogen Bond-assisted H-aggregate Formation: The ODIN Case Francesco Bertocchi, Danilo Marchetti, Sandra Doria, Mariangela di Donato, Cristina Sissa, Mauro Gemmi, Enrico Dalcanale, Roberta Pinalli, Andrea Lapini Chemistry A European Journal, 2024 The current work focuses on the investigation of two functionalized naphthyridine derivatives, namely ODIN‐EtPh and ODIN‐But, to gain insights into the hydrogen bond‐assisted H‐aggregate formation and its impact on the optical properties of ODIN molecules. By employing a combination of X‐ray and electron crystallography, absorption and emission spectroscopy, time resolved fluorescence and ultrafast pump‐probe spectroscopy (visible and infrared) we unravel the correlation between the structure and light‐matter response, with a particular emphasis on the influence of the polarity of the surrounding environment. Our experimental results and simulations confirm that in polar and good hydrogen‐bond acceptor solvents (DMSO), the formation of dimers for ODIN derivatives is strongly inhibited. The presence of a phenyl group linked to the ureidic unit favors the folding of ODIN derivatives (forming an intramolecular hydrogen bond) leading to the stabilization of a charge‐transfer excited state which almost completely quenches its fluorescence emission. In solvents with a poor aptitude for forming hydrogen bonds, the formation of dimers is favored and gives rise to H aggregates, with a consequent considerable reduction in the fluorescence emission. The urea‐bound phenyl group furtherly stabilizes the dimers in chloroform.
Solid state solvation: a fresh view Brunella Bardi, Davide Giavazzi, Elena Ferrari, Alessandro Iagatti, Mariangela Di Donato, D. K. Andrea Phan Huu, Francesco Di Maiolo, Cristina Sissa, Matteo Masino, Andrea Lapini, Anna Painelli Materials Horizons, 2023 The static and dynamic dielectric properties of amorphous matrices of interest for use in OLEDs are addressed via a careful experimental and theoretical analysis of Raman and time-resolved emission spectra of simple dyes dispersed in the matrix of interest.
Amyloidogenic and non-amyloidogenic molten globule conformation of β-lactoglobulin in self-crowded regime Sara Venturi, Barbara Rossi, Mariagrazia Tortora, Renato Torre, Andrea Lapini, Paolo Foggi, Marco Paolantoni, Sara Catalini International Journal of Biological Macromolecules, 2023 Molecular insights on the β-lactoglobulin thermal unfolding and aggregation are derived from FTIR and UV Resonance Raman (UVRR) investigations. We propose an in situ and in real-time approach that thanks to the identification of specific spectroscopic markers can distinguish the two different unfolding pathways pursued by β-lactoglobulin during the conformational transition from the folded to the molten globule state, as triggered by the pH conditions. For both the investigated pH values (1.4 and 7.5) the greatest conformational variation of β-lactoglobulin occurs at 80 °C and a high degree of structural reversibility after cooling is observed. In acidic condition β-lactoglobulin exposes to the solvent its hydrophobic moieties in a much higher extent than in neutral solution, resulting on a highly open conformation. Moving from the diluted to the self-crowded regime, the solution pH and consequently the different molten globule conformation select the amyloid or non-amyloid aggregation pathway. At acidic condition the amyloid aggregates form during the heating cycle leading to the formation of transparent hydrogel. On the contrary, in neutral condition the amyloid aggregates never form. Information on the secondary structure conformational change of β-lactoglobulin and the formation of amyloid aggregates are obtained by FTIR spectroscopy and are related to the information of the structural changes localized around the aromatic amino acid sites by UVRR technique. Our results highlight a strong involvement of the chain portions where tryptophan is located on the formation of amyloid aggregates.
Au-Coated Ni80Fe20 Submicron Magnetic Nanodisks: Interactions With Tumor Cells Carla Divieto, Gabriele Barrera, Federica Celegato, Giancarlo D'Agostino, Marco Di Luzio, Marco Coïsson, Andrea Lapini, Leonardo Mortati, Massimo Zucco, Stefano Pavarelli, Maria P. Sassi, Paola Tiberto Frontiers in Nanotechnology, 2020
Free volume and dynamics in a lipid bilayer Beatrice Gironi, Andrea Lapini, Elena Ragnoni, Chiara Calvagna, Marco Paolantoni, Assunta Morresi, Paola Sassi Physical Chemistry Chemical Physics, 2019
Shedding Light on the Photoisomerization Pathway of Donor-Acceptor Stenhouse Adducts Mariangela Di Donato, Michael M. Lerch, Andrea Lapini, Adèle D. Laurent, Alessandro Iagatti, Laura Bussotti, Svante P. Ihrig, Miroslav Medved’, Denis Jacquemin, Wiktor Szymański, Wybren Jan Buma, Paolo Foggi, Ben L. Feringa Journal of the American Chemical Society, 2017
Ultrafast resonance energy transfer in the umbelliferone-alizarin bichromophore Andrea Lapini, Pierangelo Fabbrizzi, Matteo Piccardo, Mariangela di Donato, Luisa Lascialfari, Paolo Foggi, Stefano Cicchi, Malgorzata Biczysko, Ivan Carnimeo, Fabrizio Santoro, Chiara Cappelli, Roberto Righini Physical Chemistry Chemical Physics, 2014
In 2020 the project Visco3DCell (development of a non-Invasive methodology to characterize Viscoelastic properties of 3D cell cultures) proposed by Andrea has been financed by the Cassa di Risparmio di Torino private foundation.
