Rosa Giugliano, Carla Zannella, Annalisa Chianese, Clementina Acconcia, Alessandra Monti, Roberta Della Marca, Ugo Pagnini, Serena Montagnaro, Nunzianna Doti, Carla Isernia, Massimiliano Galdiero, Filomena Fiorito, Luigi Russo, Valentina Iovane, Anna De Filippis
{"title":"抗兽医疱疹病毒的潘汀衍生肽:活性和结构表征。","authors":"Rosa Giugliano, Carla Zannella, Annalisa Chianese, Clementina Acconcia, Alessandra Monti, Roberta Della Marca, Ugo Pagnini, Serena Montagnaro, Nunzianna Doti, Carla Isernia, Massimiliano Galdiero, Filomena Fiorito, Luigi Russo, Valentina Iovane, Anna De Filippis","doi":"10.1002/cmdc.202500333","DOIUrl":null,"url":null,"abstract":"<p><p>Animal viral infections represent a growing public health concern, as animals serve as reservoirs for pathogens, threatening food safety, biodiversity, and human health. In response, novel antiviral strategies are urgently needed. This study investigates the antiviral activity and structural properties of two antimicrobial peptides, pantinin-1 and pantinin-2, both derived from the venom of the scorpion Pandinus imperator, against caprine herpesvirus 1 (CpHV-1) and bovine herpesvirus 1 (BoHV-1). The results obtained from the plaque reduction assay and the quantitative real-time polymerase chain reaction (PCR) indicate that synthetic pantinin-mimetic peptides exhibited potent antiviral effects at concentrations ranging from 6-25 µM, impairing viral infectivity through direct virucidal action and inhibition of the viral entry and fusion with host cell. To characterize their structural behavior, nuclear magnetic resonance spectroscopy is performed in aqueous and membrane-mimetic environments (trifluoroethanol (TFE)/H<sub>2</sub>O). In aqueous solution, both peptides predominantly adopted random coil conformations, with pantinin-2 showing greater secondary structure propensity. In TFE/H<sub>2</sub>O, both peptides transitioned to α-helical structures, which are often associated with membrane interaction and antiviral activity. These findings demonstrate that pantinin-1 and pantinin-2 possess promising antiviral properties, supporting their potential development as therapeutic agents against herpesviruses and other animal viral infections.</p>","PeriodicalId":147,"journal":{"name":"ChemMedChem","volume":" ","pages":"e202500333"},"PeriodicalIF":3.4000,"publicationDate":"2025-09-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Pantinin-Derived Peptides against Veterinary Herpesviruses: Activity and Structural Characterization.\",\"authors\":\"Rosa Giugliano, Carla Zannella, Annalisa Chianese, Clementina Acconcia, Alessandra Monti, Roberta Della Marca, Ugo Pagnini, Serena Montagnaro, Nunzianna Doti, Carla Isernia, Massimiliano Galdiero, Filomena Fiorito, Luigi Russo, Valentina Iovane, Anna De Filippis\",\"doi\":\"10.1002/cmdc.202500333\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Animal viral infections represent a growing public health concern, as animals serve as reservoirs for pathogens, threatening food safety, biodiversity, and human health. 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In aqueous solution, both peptides predominantly adopted random coil conformations, with pantinin-2 showing greater secondary structure propensity. In TFE/H<sub>2</sub>O, both peptides transitioned to α-helical structures, which are often associated with membrane interaction and antiviral activity. 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Pantinin-Derived Peptides against Veterinary Herpesviruses: Activity and Structural Characterization.
Animal viral infections represent a growing public health concern, as animals serve as reservoirs for pathogens, threatening food safety, biodiversity, and human health. In response, novel antiviral strategies are urgently needed. This study investigates the antiviral activity and structural properties of two antimicrobial peptides, pantinin-1 and pantinin-2, both derived from the venom of the scorpion Pandinus imperator, against caprine herpesvirus 1 (CpHV-1) and bovine herpesvirus 1 (BoHV-1). The results obtained from the plaque reduction assay and the quantitative real-time polymerase chain reaction (PCR) indicate that synthetic pantinin-mimetic peptides exhibited potent antiviral effects at concentrations ranging from 6-25 µM, impairing viral infectivity through direct virucidal action and inhibition of the viral entry and fusion with host cell. To characterize their structural behavior, nuclear magnetic resonance spectroscopy is performed in aqueous and membrane-mimetic environments (trifluoroethanol (TFE)/H2O). In aqueous solution, both peptides predominantly adopted random coil conformations, with pantinin-2 showing greater secondary structure propensity. In TFE/H2O, both peptides transitioned to α-helical structures, which are often associated with membrane interaction and antiviral activity. These findings demonstrate that pantinin-1 and pantinin-2 possess promising antiviral properties, supporting their potential development as therapeutic agents against herpesviruses and other animal viral infections.
期刊介绍:
Quality research. Outstanding publications. With an impact factor of 3.124 (2019), ChemMedChem is a top journal for research at the interface of chemistry, biology and medicine. It is published on behalf of Chemistry Europe, an association of 16 European chemical societies.
ChemMedChem publishes primary as well as critical secondary and tertiary information from authors across and for the world. Its mission is to integrate the wide and flourishing field of medicinal and pharmaceutical sciences, ranging from drug design and discovery to drug development and delivery, from molecular modeling to combinatorial chemistry, from target validation to lead generation and ADMET studies. ChemMedChem typically covers topics on small molecules, therapeutic macromolecules, peptides, peptidomimetics, and aptamers, protein-drug conjugates, nucleic acid therapies, and beginning 2017, nanomedicine, particularly 1) targeted nanodelivery, 2) theranostic nanoparticles, and 3) nanodrugs.
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