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29 results on '"Luzi, Carla"'

6. Concurrent RAS and RAS/BRAF V600E variants in colorectal cancer: more frequent than expected?

Author

Zelli, Veronica, Parisi, Alessandro, Patruno, LEONARDO VALERIO, Katia, Cannita, Ficorella, Corrado, Luzi, Carla, Compagnoni, Chiara, Zazzeroni, Francesca, Alesse, Edoardo, and Tessitore, Alessandra

Subjects
concurrent RAS/BRAF variants, colorectal cancer, concurrent RAS/BRAF variants, case report, mutation frequency, Q9 clinical–pathological features, Q9 clinical–pathological features, case report, colorectal cancer, mutation frequency
Published
2022

16. Proteomic Analysis of Quercetin-Treated K562 Cells

Author

Brisdelli, Fabrizia, primary, Di Francesco, Laura, additional, Giorgi, Alessandra, additional, Lizzi, Anna Rita, additional, Luzi, Carla, additional, Mignogna, Giuseppina, additional, Bozzi, Argante, additional, and Schininà, M. Eugenia, additional

Published
2019
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17. Tebuconazole and Econazole Act Synergistically in Mediating Mitochondrial Stress, Energy Imbalance, and Sequential Activation of Autophagy and Apoptosis in Mouse Sertoli TM4 Cells: Possible Role of AMPK/ULK1 Axis

Author

Petricca, Sabrina, primary, Flati, Vincenzo, additional, Celenza, Giuseppe, additional, Di Gregorio, Jacopo, additional, Lizzi, Anna Rita, additional, Luzi, Carla, additional, Cristiano, Loredana, additional, Cinque, Benedetta, additional, Rossi, Gianna, additional, Festuccia, Claudio, additional, and Iorio, Roberto, additional

Published
2019
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18. Propriétés structurales de la craboline, un peptide antimicrobien naturel

Author

Aschi, Massimiliano, Bozzi, Argante, Luzi, Carla, Bouchemal, Nadia, Sette, Marco, Dipartimento di Chimica, Ingegneria Chimica e Materiali, Università degli Studi dell'Aquila (UNIVAQ), Chimie, Structures et Propriétés de Biomatériaux et d'Agents Thérapeutiques (CSPBAT), and Université Paris 13 (UP13)-Institut Galilée-Université Sorbonne Paris Cité (USPC)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)

Subjects
[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biophysics
Abstract

International audience; A joint application of experimental and computational approaches has revealed the exceptionally high attitude of crabrolin, a 13-residue peptide with sequence FLPLILRKIVTAL-NH2, to adopt alpha-helix conformation not only in membrane-mimicking solvents but also in the presence of a not negligible amount of water. Our study shows that this propensity essentially resides in the intrinsic thermodynamic stability of alpha-helix conformation whose kinetic stability is drastically reduced in water solvent. Our analysis suggest that this is due to two effects enhanced by water; a more local effect consisting of the demolition of intra-peptide H-bonds, essential for the alpha-helix formation, and a bulk-electrostatic-effect favoring conformational states more polar than alpha-helix.

Published
2017

22. pH-dependent disruption ofEscherichia coliATCC 25922 and model membranes by the human antimicrobial peptides hepcidin 20 and 25

Author

Maisetta, Giuseppantonio, primary, Vitali, Alberto, additional, Scorciapino, Mariano A., additional, Rinaldi, Andrea C., additional, Petruzzelli, Raffaele, additional, Brancatisano, Franca L., additional, Esin, Semih, additional, Stringaro, Annarita, additional, Colone, Marisa, additional, Luzi, Carla, additional, Bozzi, Argante, additional, Campa, Mario, additional, and Batoni, Giovanna, additional

Published
2013
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24. Interaction of Antimicrobial Peptide Temporin L with Lipopolysaccharide In Vitro and in Experimental Rat Models of Septic Shock Caused by Gram-Negative Bacteria

Author

Giacometti, Andrea, primary, Cirioni, Oscar, additional, Ghiselli, Roberto, additional, Mocchegiani, Federico, additional, Orlando, Fiorenza, additional, Silvestri, Carmela, additional, Bozzi, Argante, additional, Di Giulio, Antonio, additional, Luzi, Carla, additional, Mangoni, Maria Luisa, additional, Barra, Donatella, additional, Saba, Vittorio, additional, Scalise, Giorgio, additional, and Rinaldi, Andrea C., additional

Published
2006
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26. P-113 Peptide: New experimental evidences on its biological activity and conformational insights from molecular dynamics simulations.

Author

Giampaolo, Alessia, Luzi, Carla, Casciaro, Bruno, Bozzi, Argante, Luisa Mangoni, Maria, and Aschi, Massimiliano

Abstract

ABSTRACT In this article, we report novel and additional results, both experimental and computational, obtained in our laboratories on the peptide P-113. In particular, our experimental results indicate that this peptide is endowed with a high target-cell selectivity towards yeast species, suggesting its potential development as a new drug against oral microbial infections. To provide additional structural insights, we performed several Molecular Dynamics simulations in different conditions. Results suggest that P-113 is a rather compact species presumably because of its highly charged state as emerged from the dramatic increase of internal fluctuation occurring upon point-mutation. The peptide turns out to adopt, in water, a beta-hairpin-like conformation and, in a more hydrophobic environment, is found to be in a (probably slow) equilibrium between α-helix and hairpin conformations. Complexation with Zn2+ induces a drastic mechanical stabilization, which prevents any conformational organization of the peptide into a biologically active state. © 2013 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 102: 159-167, 2014. [ABSTRACT FROM AUTHOR]

Published
2014
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28. Proteomic Analysis of Quercetin-Treated K562 Cells.

Author

Brisdelli, Fabrizia, Di Francesco, Laura, Giorgi, Alessandra, Lizzi, Anna Rita, Luzi, Carla, Mignogna, Giuseppina, Bozzi, Argante, and Schininà, M. Eugenia

Subjects
CHRONIC myeloid leukemia, RNA metabolism, RADIOLABELING, LIPID metabolism, STABLE isotopes, PROTEOMICS
Abstract

Among natural products under investigation for their additive potential in cancer prevention and treatment, the flavonoid quercetin has received attention for its effects on the cell cycle arrest and apoptosis. In the past, we addressed this issue in K562 cells, a cellular model of the human chronic myeloid leukemia. Here, we applied stable isotope labeling by amino acids in cell culture (SILAC) proteomics with the aim to increase knowledge on the regulative and metabolic pathways modulated by quercetin in these cells. After 24 h of quercetin treatment, we observed that apoptosis was not completely established, thus we selected this time range to capture quantitative data. As a result, we were able to achieve a robust identification of 1703 proteins, and to measure fold changes between quercetin-treated and untreated cells for 1206 proteins. Through a bioinformatics functional analysis on a subset of 112 proteins, we propose that the apoptotic phenotype of K562 cells entails a significant modulation of the translational machinery, RNA metabolism, antioxidant defense systems, and enzymes involved in lipid metabolism. Finally, we selected eight differentially expressed proteins, validated their modulated expression in quercetin-treated K562 cells, and discussed their possible role in flavonoid cytotoxicity. This quantitative profiling, performed for the first time on this type of tumor cells upon treatment with a flavonoid, will contribute to revealing the molecular basis of the multiplicity of the effects selectively exerted by quercetin on K562 cells. [ABSTRACT FROM AUTHOR]

Published
2020
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29. P-113 peptide: New experimental evidences on its biological activity and conformational insights from molecular dynamics simulations.

Author

Di Giampaolo A, Luzi C, Casciaro B, Bozzi A, Mangoni ML, and Aschi M

Subjects
Anti-Infective Agents pharmacology, Bacteria drug effects, Microbial Sensitivity Tests, Protein Structure, Secondary, Solutions, Thermodynamics, Time Factors, Trifluoroethanol chemistry, Water chemistry, Yeasts drug effects, Molecular Dynamics Simulation, Peptides chemistry, Peptides pharmacology
Abstract

In this article, we report novel and additional results, both experimental and computational, obtained in our laboratories on the peptide P-113. In particular, our experimental results indicate that this peptide is endowed with a high target-cell selectivity towards yeast species, suggesting its potential development as a new drug against oral microbial infections. To provide additional structural insights, we performed several Molecular Dynamics simulations in different conditions. Results suggest that P-113 is a rather compact species presumably because of its highly charged state as emerged from the dramatic increase of internal fluctuation occurring upon point-mutation. The peptide turns out to adopt, in water, a beta-hairpin-like conformation and, in a more hydrophobic environment, is found to be in a (probably slow) equilibrium between α-helix and hairpin conformations. Complexation with Zn(2+) induces a drastic mechanical stabilization, which prevents any conformational organization of the peptide into a biologically active state., (Copyright © 2013 Wiley Periodicals, Inc.)

Published
2014
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