Antifungal activity of designed α-helical antimicrobial peptides

Xu, Ruicheng; Tang, Jing; Hadianamrei, Roja; Liu, Suyu; Lv, Songwei; You, Rongrong; Pan, Fang; Zhang, Peng; Wang, Nan; Cai, Zhiqiang; Zhao, Xiaoyong

doi:10.1039/d2bm01797k

Cited by 9 publications

(2 citation statements)

References 60 publications

(93 reference statements)

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“…Antimicrobial peptides (AMPs) widely exist in the innate immune systems of all kingdoms of different species, which can attack pathogens through nonreceptor-mediated membrane damage. 4 Broad-spectrum activities, multiple action mechanisms (including a membrane-penetrating and a nonmembranepenetrating mechanism), and difficult-to-generate drug resistance render AMPs ideal antimicrobial agents. 5 However, inadequate physicochemical and physiological stability, high cytotoxicity, and cost severely restrict their clinical application.…”

Section: ■ Introductionmentioning

confidence: 99%

Engineered Peptides Harboring Cation Motifs Against Multidrug-Resistant Bacteria

Shang,

Chen,

Sun

et al. 2024

ACS Appl. Mater. Interfaces

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Multidrug-resistant (MDR) pathogens pose a serious threat to the health and life of humans, necessitating the development of new antimicrobial agents. Herein, we develop and characterize a panel of nine amino acid peptides with a cation end motif. Bioactivity analysis revealed that the short peptide containing "RWWWR" as a central motif harboring mirror structure "KXR" unit displayed not only high activity against MDR planktonic bacteria but also a clearance rate of 92.33% ± 0.58% against mature biofilm. Mechanically, the target peptide (KLR) killed pathogens by excessively accumulating reactive oxygen species and physically disrupting membranes, thereby enhancing its robustness for controlling drug resistance. In the animal model of sepsis infection by MDR bacteria, the peptide KLR exhibited strong therapeutic effects. Collectively, this study provided the dominant structure of short antimicrobial peptides (AMPs) to replenish our arsenals for combating bacterial infections and illustrated what could be harnessed as a new agent for fighting MDR bacteria.

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Section: ■ Introductionmentioning

confidence: 99%

Engineered Peptides Harboring Cation Motifs Against Multidrug-Resistant Bacteria

Shang,

Chen,

Sun

et al. 2024

ACS Appl. Mater. Interfaces

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“…It is possible to search for suitable materials for the peptide functionalization to synthesize SRPNs can undergo behavioural changes triggered by the conditions such as pH, temperature, enzymes, reactive oxygen species (ROS), and light [ [13] , [14] , [15] , [16] ]. The stimuli-responsive properties are important for biomedical applications such as drug delivery, tumor diagnostics, bioimaging, and biosensors [ [17] , [18] , [19] ].…”

Section: Introductionmentioning

confidence: 99%

Stimuli-responsive peptide assemblies: Design, self-assembly, modulation, and biomedical applications

Mu,

Zhu,

Abdulmalik

et al. 2024

Bioactive Materials

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Characterization and functional analysis of gerbera plant defensin (PDF) genes reveal the role of GhPDF2.4 in defense against the root rot pathogen Phytophthora cryptogea

Cheng,

Wu,

Zhang

2024

aBIOTECH

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Gerbera (Gerbera hybrida), a major fresh cut flower crop, is very susceptible to root rot disease. Although plant defensins (PDFs), a major group of plant antimicrobial peptides, display broad-spectrum antifungal and antibacterial activities, PDF genes in gerbera have not been systematically characterized. Here, we identified and cloned nine PDF genes from gerbera and divided them into two classes based on phylogenetic analysis. Most Class I GhPDF genes were highly expressed in petioles, whereas all Class II GhPDF genes were highly expressed in roots. Phytophthora cryptogea inoculation strongly upregulated all Class II GhPDF genes in roots and upregulated all Class I GhPDF genes in petioles. Transient overexpression of GhPDF1.5 and GhPDF2.4 inhibited P. cryptogea infection in tobacco (Nicotiana benthamiana) leaves. Transient overexpression of GhPDF2.4, but not GhPDF1.5, significantly upregulated ACO and LOX gene expression in tobacco leaves, indicating that overexpressing GhPDF2.4 activated the jasmonic acid/ethylene defense pathway and that the two types of GhPDFs have different modes of action. Prokaryotically expressed recombinant GhPDF2.4 inhibited mycelial growth and delayed the hyphal swelling of P. cryptogea, in vitro, indicating that GhPDF2.4 is a morphogenetic defensin. Moreover, the addition of GhPDF2.4 to plant culture medium alleviated the root rot symptoms of in vitro-grown gerbera seedlings and greatly reduced pathogen titer in P. cryptogea-inoculated gerbera roots in the early stages of treatment. Our study provides a basis for the use of GhPDFs, especially GhPDF2.4, for controlling root rot disease in gerbera.

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Antifungal activity of designed α-helical antimicrobial peptides

Abstract: Antimicrobial resistance (AMR) has become a major global health concern prompting the quest for new antibiotics with higher efficiency and less proneness to drug resistance. Antimicrobial peptides (AMPs) offer such...

Cited by 9 publications

References 60 publications

Engineered Peptides Harboring Cation Motifs Against Multidrug-Resistant Bacteria

Engineered Peptides Harboring Cation Motifs Against Multidrug-Resistant Bacteria

Stimuli-responsive peptide assemblies: Design, self-assembly, modulation, and biomedical applications

Characterization and functional analysis of gerbera plant defensin (PDF) genes reveal the role of GhPDF2.4 in defense against the root rot pathogen Phytophthora cryptogea

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