a1e05b6c418b0711cb207a26af2d1ad4 pmc_11125377.pdf 94517b1766bc6fbfc0aa745da2d3f3bfce00220a pmc_11125377.pdf b5f1c388d0310692ac2e463dd311c0d61e2d1857875a7a1fd528b29f86dce8be pmc_11125377.pdf Title: Plant Protease Inhibitors as Emerging Antimicrobial Peptide Agents: A Comprehensive Review Subject: Antimicrobial peptides (AMPs) are important mediator molecules of the innate defense mechanisms in a wide range of living organisms, including bacteria, mammals, and plants. Among them, peptide protease inhibitors (PPIs) from plants play a central role in their defense mechanisms by directly attacking pathogens or by modulating the plant’s defense response. The growing prevalence of microbial resistance to currently available antibiotics has intensified the interest concerning these molecules as novel antimicrobial agents. In this scenario, PPIs isolated from a variety of plants have shown potential in inhibiting the growth of pathogenic bacteria, protozoans, and fungal strains, either by interfering with essential biochemical or physiological processes or by altering the permeability of biological membranes of invading organisms. Moreover, these molecules are active inhibitors of a range of proteases, including aspartic, serine, and cysteine types, with some showing particular efficacy as trypsin and chymotrypsin inhibitors. In this review, we provide a comprehensive analysis of the potential of plant-derived PPIs as novel antimicrobial molecules, highlighting their broad-spectrum antimicrobial efficacy, specificity, and minimal toxicity. These natural compounds exhibit diverse mechanisms of action and often multifunctionality, positioning them as promising molecular scaffolds for developing new therapeutic antibacterial agents. Keywords: plant protease inhibitors; antibacterial compounds; antimicrobial activity; antimicrobial peptides; antibiotic resistance; antifungal agents; cysteine-rich peptides Author: Mónica G. Parisi, Brenda Ozón, Sofía M. Vera González, Javier García-Pardo and Walter David Obregón Creator: LaTeX with hyperref Producer: pdfTeX-1.40.25 CreationDate: Mon Apr 29 05:55:01 2024 CEST ModDate: Mon Apr 29 05:59:34 2024 CEST Custom Metadata: no Metadata Stream: no Tagged: no UserProperties: no Suspects: no Form: none JavaScript: no Pages: 15 Encrypted: no Page size: 595.276 x 841.89 pts (A4) Page rot: 0 File size: 1678019 bytes Optimized: no PDF version: 1.7 name type encoding emb sub uni object ID ------------------------------------ ----------------- ---------------- --- --- --- --------- PRJKGQ+VnURWPalladioL-Bold Type 1 Custom yes yes yes 10 0 FKIXHZ+URWPalladioL-Bold Type 1 Custom yes yes yes 16 0 YKQOKK+URWPalladioL-Roma Type 1 Custom yes yes yes 22 0 LVQOGM+URWPalladioL-Ital Type 1 Custom yes yes yes 27 0 PSUYZB+VnURWPalladioL Type 1 Custom yes yes yes 32 0 IAFAOG+TimesNewRomanPS-BoldItalicMT Type 1C WinAnsi yes yes no 49 0 LEVXPH+EURM10 Type 1 Builtin yes yes yes 72 0 FGKEHB+PalatinoLinotype,Bold TrueType WinAnsi yes yes no 83 0 FGKEHC+PalatinoLinotype CID TrueType Identity-H yes yes yes 86 0 FGKEHD+PalatinoLinotype TrueType WinAnsi yes yes no 92 0 FGKEHF+PalatinoLinotype,Italic TrueType WinAnsi yes yes no 95 0 FGKEME+PalatinoLinotype TrueType MacRoman yes yes no 98 0 FGKEHB+PalatinoLinotype,Bold TrueType WinAnsi yes yes no 109 0 FGKEHC+PalatinoLinotype CID TrueType Identity-H yes yes yes 112 0 FGKEHD+PalatinoLinotype TrueType WinAnsi yes yes no 118 0 FGKEHF+PalatinoLinotype,Italic TrueType WinAnsi yes yes no 121 0 FGKEME+PalatinoLinotype TrueType MacRoman yes yes no 124 0 EILUJF+CMSY10 Type 1 Builtin yes yes yes 131 0 FGKEHB+PalatinoLinotype,Bold TrueType WinAnsi yes yes no 139 0 FGKEHC+PalatinoLinotype CID TrueType Identity-H yes yes yes 142 0 FGKEHD+PalatinoLinotype TrueType WinAnsi yes yes no 148 0 FGKEHF+PalatinoLinotype,Italic TrueType WinAnsi yes yes no 151 0 FGKEME+PalatinoLinotype TrueType MacRoman yes yes no 154 0 FGKGDM+TimesNewRoman,Bold CID TrueType Identity-H yes yes yes 157 0 FGKEHB+PalatinoLinotype,Bold TrueType WinAnsi yes yes no 170 0 FGKEHC+PalatinoLinotype CID TrueType Identity-H yes yes yes 173 0 FGKEHD+PalatinoLinotype TrueType WinAnsi yes yes no 179 0 FGKEHF+PalatinoLinotype,Italic TrueType WinAnsi yes yes no 182 0 FGKEME+PalatinoLinotype TrueType MacRoman yes yes no 185 0 Jhove (Rel. 1.28.0, 2023-05-18) Date: 2024-07-13 02:36:57 CEST RepresentationInformation: pmc_11125377.pdf ReportingModule: PDF-hul, Rel. 1.12.4 (2023-03-16) LastModified: 2024-06-13 02:35:31 CEST Size: 1678019 Format: PDF Version: 1.7 Status: Well-Formed and valid SignatureMatches: PDF-hul MIMEtype: application/pdf PDFMetadata: Objects: 610 FreeObjects: 1 IncrementalUpdates: 0 DocumentCatalog: PageLayout: SinglePage PageMode: UseNone Outlines: Item: Title: Introduction Destination: section.1 Item: Title: Antimicrobial Peptides (AMPs) Destination: section.2 Item: Title: Mechanism of Antimicrobial Action of Plant AMPs Destination: section.3 Item: Title: Peptide Protease Inhibitors (PPIs) Derived from Plants Destination: section.4 Item: Title: Plant-Derived Peptide Protease Inhibitors with Antimicrobial Properties Destination: section.5 Children: Item: Title: Plant Protease Inhibitors with Antibacterial Activity Destination: subsection.5.1 Item: Title: Plant Protease Inhibitors with Antifungal Activity Destination: subsection.5.2 Item: Title: Concluding Remarks and Future Perspectives Destination: section.6 Item: Title: References Destination: section.7 Info: Title: Plant Protease Inhibitors as Emerging Antimicrobial Peptide Agents: A Comprehensive Review Author: Mónica G. Parisi, Brenda Ozón, Sofía M. Vera González, Javier García-Pardo and Walter David Obregón Subject: Antimicrobial peptides (AMPs) are important mediator molecules of the innate defense mechanisms in a wide range of living organisms, including bacteria, mammals, and plants. Among them, peptide protease inhibitors (PPIs) from plants play a central role in their defense mechanisms by directly attacking pathogens or by modulating the plant’s defense response. The growing prevalence of microbial resistance to currently available antibiotics has intensified the interest concerning these molecules as novel antimicrobial agents. In this scenario, PPIs isolated from a variety of plants have shown potential in inhibiting the growth of pathogenic bacteria, protozoans, and fungal strains, either by interfering with essential biochemical or physiological processes or by altering the permeability of biological membranes of invading organisms. Moreover, these molecules are active inhibitors of a range of proteases, including aspartic, serine, and cysteine types, with some showing particular efficacy as trypsin and chymotrypsin inhibitors. In this review, we provide a comprehensive analysis of the potential of plant-derived PPIs as novel antimicrobial molecules, highlighting their broad-spectrum antimicrobial efficacy, specificity, and minimal toxicity. These natural compounds exhibit diverse mechanisms of action and often multifunctionality, positioning them as promising molecular scaffolds for developing new therapeutic antibacterial agents. 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