Structural insights on the selective interaction of the histidine-rich piscidin antimicrobial peptide Of-Pis1 with membranes

Bischetti, Martina; Alaimo, Nadine; Nardelli, Francesca; Punzi, Pasqualina; Amariei, Cristi; Ingenito, Raffaele; Musco, Giovana; Gallo, Mariana; Cicero, Daniel O.

doi:10.1016/j.bbamem.2022.184080

Cited by 5 publications

(9 citation statements)

References 71 publications

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“…Although the exact mechanism of action of peptides is not yet clear, all piscidin peptides studied might have membrane-binding and disrupting properties, leading to the formation of transient pores or channels in the membrane and ultimately microbial death [63]. The hydrophobic component of piscidin peptides can also result in partial or complete penetration into the lipid bilayer, resulting in the disruption, destruction, or fragmentation of the microbial membrane [38]. Several data suggest the possibility that these AMPs may not only create pores but also interfere with cellular processes such as protein and nucleic acid synthesis and enzymatic reactions.…”

Section: Mechanisms Of Actionmentioning

confidence: 99%

“…The bacteriostatic and bactericidal effects of Pleurocidin are quite broad (Table 3) but have been shown to be somewhat attenuated against Leucothrix mucor, Pseudomonas aeruginosa, and Serratia marcescens [73]. The orientation and conformation of peptides in lipidic environments are also affected by the peptide to lipid molar ratio [38]. When the peptide-lipid ratio is low, the peptide binds perpendicular to the membrane.…”

Section: Mechanisms Of Actionmentioning

confidence: 99%

“…Because piscidins are naturally produced by fish, they may be less likely to cause adverse effects in humans than synthetic antimicrobial agents [37]. However, more research is needed to fully understand the potential benefits and limitations of using piscidins in humans [38].…”

Section: Introductionmentioning

confidence: 99%

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Teleost Piscidins—In Silico Perspective of Natural Peptide Antibiotics from Marine Sources

et al. 2023

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Fish, like all other animals, are exposed to constant contact with microbes, both on their skin and on the surfaces of their respiratory and digestive systems. Fish have a system of non-specific immune responses that provides them with initial protection against infection and allows them to survive under normal conditions despite the presence of these potential invaders. However, fish are less protected against invading diseases than other marine vertebrates because their epidermal surface, composed primarily of living cells, lacks the keratinized skin that serves as an efficient natural barrier in other marine vertebrates. Antimicrobial peptides (AMPs) are one type of innate immune protection present in all life forms. AMPs have been shown to have a broader range of biological effects than conventional antibiotics, including antibacterial, antiviral, antiprotozoal, and antifungal effects. Although other AMPs, such as defensins and hepcidins, are found in all vertebrates and are relatively well conserved, piscidins are found exclusively in Teleost fish and are not found in any other animal. Therefore, there is less information on the expression and bioactivity of piscidins than on other AMPs. Piscidins are highly effective against Gram-positive and Gram-negative bacteria that cause disease in fish and humans and have the potential to be used as pharmacological anti-infectives in biomedicine and aquaculture. To better understand the potential benefits and limitations of using these peptides as therapeutic agents, we are conducting a comprehensive study of the Teleost piscidins included in the “reviewed” category of the UniProt database using bioinformatics tools. They all have amphipathic alpha-helical structures. The amphipathic architecture of piscidin peptides and positively charged residues influence their antibacterial activity. These alpha-helices are intriguing antimicrobial drugs due to their stability in high-salt and metal environments. New treatments for multidrug-resistant bacteria, cancer, and inflammation may be inspired by piscidin peptides.

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Section: Mechanisms Of Actionmentioning

confidence: 99%

Section: Mechanisms Of Actionmentioning

confidence: 99%

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Teleost Piscidins—In Silico Perspective of Natural Peptide Antibiotics from Marine Sources

et al. 2023

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“…For this reason, the characteristic is also evaluated in different situations to increase the possibilities of using them in medical therapies. The piscidine Of-Pis1 , a recently isolated peptide from rock bream ( Oplegnathus fasciatus ), proved its potential in the test against different pathogens [ 61 ]. Of-Pis1 has a spiral arrangement only in the presence of an Escherichia coli membrane.…”

Section: Mechanisms Of Actionmentioning

confidence: 99%

“…It is vital to determine their optimum action parameters to obtain reliable results on peptides’ possible use in the pharmacological domain. Different investigations in this regard highlight this aspect [ 60 , 61 , 62 ]. Other elements, distinct in their impact on the cell membrane, influence permeability [ 63 ].…”

Section: Mechanisms Of Actionmentioning

confidence: 99%

Membrane-Active Peptides and Their Potential Biomedical Application

Gostaviceanu,

Gavrilaş,

Copolovici

et al. 2023

Pharmaceutics

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Membrane-active peptides (MAPs) possess unique properties that make them valuable tools for studying membrane structure and function and promising candidates for therapeutic applications. This review paper provides an overview of the fundamental aspects of MAPs, focusing on their membrane interaction mechanisms and potential applications. MAPs exhibit various structural features, including amphipathic structures and specific amino acid residues, enabling selective interaction with multiple membranes. Their mechanisms of action involve disrupting lipid bilayers through different pathways, depending on peptide properties and membrane composition. The therapeutic potential of MAPs is significant. They have demonstrated antimicrobial activity against bacteria and fungi, making them promising alternatives to conventional antibiotics. MAPs can selectively target cancer cells and induce apoptosis, opening new avenues in cancer therapeutics. Additionally, MAPs serve as drug delivery vectors, facilitating the transport of therapeutic cargoes across cell membranes. They represent a fascinating class of biomolecules with significant potential in basic research and clinical applications. Understanding their mechanisms of action and designing peptides with enhanced selectivity and efficacy will further expand their utility in diverse fields. Exploring MAPs holds promise for developing novel therapeutic strategies against infections, cancer, and drug delivery challenges.

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Elucidating the conformational behavior and membrane-destabilizing capability of the antimicrobial peptide ecPis-4s

de Souza,

Nunes,

Salnikov

et al. 2025

Biophysical Chemistry

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Structural insights on the selective interaction of the histidine-rich piscidin antimicrobial peptide Of-Pis1 with membranes

Cited by 5 publications

References 71 publications

Teleost Piscidins—In Silico Perspective of Natural Peptide Antibiotics from Marine Sources

Teleost Piscidins—In Silico Perspective of Natural Peptide Antibiotics from Marine Sources

Membrane-Active Peptides and Their Potential Biomedical Application

Elucidating the conformational behavior and membrane-destabilizing capability of the antimicrobial peptide ecPis-4s

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