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48 results on '"Gogliettino, Marta"'

6. Antimicrobial activity, membrane interaction and structural features of short arginine-rich antimicrobial peptides

Author

Agrillo, Bruna, primary, Porritiello, Alessandra, additional, Gratino, Lorena, additional, Balestrieri, Marco, additional, Proroga, Yolande Therese, additional, Mancusi, Andrea, additional, Cozzi, Loredana, additional, Vicenza, Teresa, additional, Dardano, Principia, additional, Miranda, Bruno, additional, Escribá, Pablo V., additional, Gogliettino, Marta, additional, and Palmieri, Gianna, additional

Published
2023
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9. Recombinant Expression of Archaeal Superoxide Dismutases in Plant Cell Cultures: A Sustainable Solution with Potential Application in the Food Industry

Author

Gogliettino, Marta, primary, Arciello, Stefania, additional, Cillo, Fabrizio, additional, Carluccio, Anna Vittoria, additional, Palmieri, Gianna, additional, Apone, Fabio, additional, Ambrosio, Rosa Luisa, additional, Anastasio, Aniello, additional, Gratino, Lorena, additional, Carola, Antonietta, additional, and Cocca, Ennio, additional

Published
2022
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19. Extending the Shelf-Life of Meat and Dairy Products via PET-Modified Packaging Activated With the Antimicrobial Peptide MTP1

Author

Gogliettino, Marta, primary, Balestrieri, Marco, additional, Ambrosio, Rosa Luisa, additional, Anastasio, Aniello, additional, Smaldone, Giorgio, additional, Proroga, Yolande T. R., additional, Moretta, Rosalba, additional, Rea, Ilaria, additional, De Stefano, Luca, additional, Agrillo, Bruna, additional, and Palmieri, Gianna, additional

Published
2020
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23. Small Synthetic Peptides Bioconjugated to Hybrid Gold Nanoparticles Destroy Potentially Deadly Bacteria at Submicromolar Concentrations

Author

Palmieri, Gianna, primary, Tatè, Rosarita, additional, Gogliettino, Marta, additional, Balestrieri, Marco, additional, Rea, Ilaria, additional, Terracciano, Monica, additional, Proroga, Yolande Therese, additional, Capuano, Federico, additional, Anastasio, Aniello, additional, and De Stefano, Luca, additional

Published
2018
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29. Low Erythrocyte Levels of Proteasome and Acyl-Peptide Hydrolase (APEH) Activities in Alzheimer’s Disease: A Sign of Defective Proteostasis?

Author

Palmieri, Gianna, primary, Cocca, Ennio, additional, Gogliettino, Marta, additional, Valentino, Roberta, additional, Ruvo, Menotti, additional, Cristofano, Gloria, additional, Angiolillo, Antonella, additional, Balestrieri, Marco, additional, Rossi, Mosè, additional, and Di Costanzo, Alfonso, additional

Published
2017
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31. Proteasome and Acylpeptide hydrolase system: exploring an alternative strategy in cancer therapy

Author

Gogliettino, Marta

Abstract

Acylpeptide hydrolase (APEH), one of the four members of the prolyl oligopeptidase class, catalyses the removal of Nacylated amino acids from acetylated peptides and it has been postulated to play a key role in protein degradation machinery. Disruption of protein turnover has been established as an effective strategy to down-regulate the ubiquitinproteasome system (UPS) and as a promising approach in anticancer therapy. Here, we illustrate a new pathway modulating UPS and proteasome activity through inhibition of APEH. To find novel molecules able to down-regulate APEH activity, we screened a set of synthetic peptides, reproducing the reactive-site loop of a known archaeal inhibitor of APEH (SsCEI), and the conjugated linoleic acid (CLA) isomers. A 12-mer SsCEI peptide and the trans10-cis12 isomer of CLA, were identified as specific APEH inhibitors and their effects on cell-based assays were paralleled by a dose-dependent reduction of proteasome activity. Moreover, cell treatment with the individual compounds increased the cytoplasm levels of several classic hallmarks of proteasome inhibition, such as NFkappaB and misfolded or polyubiquitinylated proteins, without any cytotoxicity. Remarkably, transfection of human bronchial epithelial cells with APEH siRNA, promoted a marked accumulation of a mutant of the cystic fibrosis transmembrane conductance regulator (CFTR), herein used as a model of misfolded protein typically degraded by UPS. Our study supports a previously unrecognized role of APEH as a negative effector of proteasome activity by an unknown mechanism and opens new perspectives for the development of strategies aimed at modulation of cancer progression.

Published
2014

43. Oxidized Substrates of APEH as a Tool to Study the Endoprotease Activity of the Enzyme.

Author

Sandomenico, Annamaria, Gogliettino, Marta, Iaccarino, Emanuela, Fusco, Carmela, Caporale, Andrea, Ruvo, Menotti, Palmieri, Gianna, and Cocca, Ennio

Subjects
*ENZYMES, *PROTEOLYSIS, *C-terminal residues, *METHIONINE, *SERINE, *PROTEOLYTIC enzymes
Abstract

APEH is a ubiquitous and cytosolic serine protease belonging to the prolyl oligopeptidase (POP) family, playing a critical role in the processes of degradation of proteins through both exo- and endopeptidase events. Endopeptidase activity has been associated with protein oxidation; however, the actual mechanisms have yet to be elucidated. We show that a synthetic fragment of GDF11 spanning the region 48–64 acquires sensitivity to the endopeptidase activity of APEH only when the methionines are transformed into the corresponding sulphoxide derivatives. The data suggest that the presence of sulphoxide-modified methionines is an important prerequisite for the substrates to be processed by APEH and that the residue is crucial for switching the enzyme activity from exo- to endoprotease. The cleavage occurs on residues placed on the C-terminal side of Met(O), with an efficiency depending on the methionine adjacent residues, which thereby may play a crucial role in driving and modulating APEH endoprotease activity. [ABSTRACT FROM AUTHOR]

Published
2022
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44. New structural determinants for antimicrobial peptides?

Author

Lucia Falcigno, Gabriella D’Auria, Marco Balestrieri, Marta Gogliettino, Bruna Agrillo, Rosaria Tatè, Principia Dardano, Luigi Nicolais, Gianna Palmieri, G. Morelli, P. Grieco, M. Saviano, M. Ruvo, Falcigno, Lucia, D'Auria, Gabriella, Balestrieri, Marco, Gogliettino, Marta, Agrillo, Bruna, Tatè, Rosaria, Dardano, Principia, Nicolais, Luigi, and Palmieri, Gianna

Subjects
AMP, RiLK1, NMR, SDS
Published
2022

45. An Active Peptide-Based Packaging System to Improve the Freshness and Safety of Fish Products: A Case Study

Author

Rosa Luisa Ambrosio, Marta Gogliettino, Bruna Agrillo, Yolande T. R. Proroga, Marco Balestrieri, Lorena Gratino, Daniela Cristiano, Gianna Palmieri, Aniello Anastasio, Ambrosio, ROSA LUISA, Gogliettino, Marta, Agrillo, Bruna, Proroga, Yolande T. R., Balestrieri, Marco, Gratino, Lorena, Cristiano, Daniela, Palmieri, Gianna, and Anastasio, Aniello

Subjects
Health (social science), antimicrobial polymers, Chemical technology, spoilage, fish quality, TP1-1185, Plant Science, Health Professions (miscellaneous), Microbiology, antimicrobial peptides, food safety, fresh fish, food packaging, Food Science
Abstract

Fresh fish are highly perishable, owing mainly to their moisture content, high amount of free amino acids and polyunsaturated fatty acids. Microorganisms and chemical reactions cause the spoilage, leading to loss in quality, human health risks and a market value reduction. Therefore, the fishing industry has always been willing to explore new technologies to increase quality and safety of fish products through a decrease of the microbiological and biochemical damage. In this context, antimicrobial active packaging is one such promising solution to meet consumer demands. The main objective of this study was to evaluate the effects of an active polypropylene-based packaging functionalized with the antimicrobial peptide 1018K6 on microbial growth, physicochemical properties and the sensory attributes of raw salmon fillets. The results showed that application of 1018K6-polypropylene strongly inhibited the microbial growth of both pathogenic and specific spoilage organisms (SSOs) on fish fillets after 7 days. Moreover, salmon also kept its freshness as per volatile chemical spoilage indices (CSIs) during storage. Similar results were obtained on hamburgers of Sarda sarda performing the same analyses. This work provides further evidence that 1018K6-polymers have good potential as antimicrobial packaging for application in the food market to enhance quality and preserve the sensorial properties of fish products.

Published
2021

46. Rapid biofilm eradication of the antimicrobial peptide 1018-K6 against Staphylococcus aureus: A new potential tool to fight bacterial biofilms

Author

Marco Balestrieri, Angelo Colagiorgi, Pierluigi Aldo Di Ciccio, Marta Gogliettino, Aniello Anastasio, Gianna Palmieri, Adriana Ianieri, Rossella Festa, Colagiorgi, Angelo, Festa, Rossella, Di Ciccio, Pierluigi A., Gogliettino, Marta, Balestrieri, Marco, Palmieri, Gianna, Anastasio, Aniello, and Ianieri, Adriana

Subjects
Staphylococcus aureus, Antimicrobial peptides, Context (language use), medicine.disease_cause, 01 natural sciences, Microbiology, Food safety, 0404 agricultural biotechnology, Listeria monocytogenes, medicine, Chemistry, business.industry, 010401 analytical chemistry, Biofilm, 04 agricultural and veterinary sciences, biochemical phenomena, metabolism, and nutrition, Antimicrobial, 040401 food science, 0104 chemical sciences, Staphylococcal Food Poisoning, Foodborne pathogens, Biofilms, business, Food Science, Biotechnology
Abstract

Staphylococcal food poisoning – caused by certain enterotoxigenic staphylococci – is one of the most common worldwide foodborne diseases. In this context, bacterial biofilms on food processing plan surfaces can represent critical sources of contamination, being more resistant to cleaning and disinfection procedures. Therefore, it is important to prevent and control biofilm formation in food facilities. In the last years, antimicrobial peptides (AMPs) have emerged as promising biofilm contrasting tools. The recently developed AMP, named 1018-K6, revealed a significant bactericidal (MBC 10 μM) and biofilm-preventing efficiency (MBIC 50 μM) against a reference ATCC strain of Listeria monocytogenes and remarkable stability under different environmental conditions. In this work, a kinetic of action of 1018-K6 against two strong biofilm-producing reference strains of Staphylococcus aureus (including a methicillin-resistant S. aureus strain) and a moderate biofilm producer enterotoxigenic S. aureus isolated from cheese, was performed. The peptide showed an impressive rapid mode of action, eradicating established biofilms within few minutes. Bactericidal activity against planktonic cells and inhibition of biofilm formation were also observed. The significant properties of 1018-K6 make it a promising candidate for applications in food-safety and quality control.

Published
2020

47. In Vitro Assays for the Bifunctional Acylpeptide Hydrolase (APEH) Enzyme from Antarctic Fish.

Author

Fusco C, Agrillo B, Gogliettino M, Palmieri G, and Cocca E

Subjects
Animals, Antarctic Regions, Endopeptidases metabolism, Exopeptidases metabolism, Proteolysis, Fishes metabolism, Peptide Hydrolases metabolism
Abstract

The bifunctional enzyme acylpeptide hydrolase (APEH) is involved in important metabolic processes both as an exopeptidase and as an endopeptidase. Hence, the growing interest in the study of this protein and the need to set up in vitro assays for its characterization. This chapter describes two in vitro assays able to detect the activities of APEH, one for the exopeptidase activity and one for the endopeptidase activity. In particular, these assays have been set up on the two APEH isoforms from Antarctic fish, characterized by a distinct functionality and marked exo- and endopeptidase activities., (© 2022. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.)

Published
2022
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48. First Archaeal PEPB-Serine Protease Inhibitor from Sulfolobus solfataricus with Noncanonical Amino Acid Sequence in the Reactive-Site Loop.

Author

Palmieri G, Catara G, Saviano M, Langella E, Gogliettino M, and Rossi M

Subjects
Amino Acid Sequence, Chymotrypsin chemistry, Escherichia coli metabolism, Kinetics, Mass Spectrometry methods, Molecular Conformation, Molecular Sequence Data, Proteomics methods, Sequence Homology, Amino Acid, Serine Endopeptidases chemistry, Archaea metabolism, Catalytic Domain, Phosphatidylethanolamine Binding Protein metabolism, Sulfolobus solfataricus metabolism
Abstract

The specific inhibition of serine proteinases, which are crucial switches in many important physiological processes, is of great value both for basic research and for therapeutic applications. In this study, we report the molecular cloning of the sso0767 gene from Sulfolobus solfataricus, and the functional characterization of its product, SsCEI, which represents the first archaeal phosphatidylethanolamine-binding protein (PEBP)-serine proteinase inhibitor, reported to date. SsCEI is a monomer protein with a molecular mass of 19.0 kDa and a pI of 6.7, which is able to inhibit the serine proteases alpha-chymotrypsin and elastase with K(i) values of 0.08 and 0.1 microM, respectively. Moreover SsCEI is extremely resistant to both thermal inactivation and proteolytic attack suggesting compact folding of the protein. Within the I51 family, the archaeal inhibitor shows strong similarity to the human and murine members. The three-dimensional model of SsCEI revealed a general beta-fold and the presence of an anion-binding pocket, the hallmark of the PEBP family. Moreover SsCEI binds the cognate proteases according to a common, substrate-like standard mechanism. Point mutation experiments supported the prediction of the protease-binding site located on the surface at the C- terminal region of the protein. Interestingly, searches based on preidentified structural reactive loop motifs revealed the occurrence of a sequence (T123-N130) that is not represented in all serine-protease inhibitor families. This unique motif may provide new insights into both the inhibitor/protease binding mode and the specific biological functions of SsCEI within the PEBP family.

Published
2009
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