Binding loop of sunflower trypsin inhibitor 1 serves as a design motif for proteolysis-resistant antimicrobial peptides

Wang, Chensi; Shao, Changxuan; Fang, Yuxin; Wang, Jiajun; Dong, Na; Shan, Anshan

doi:10.1016/j.actbio.2021.01.036

Cited by 57 publications

(48 citation statements)

References 56 publications

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“…The MIC values of P19 in the presence of physiological salt concentrations increased somewhat were a little raised, especially in the presence of Na + . This is primarily arising due to the high ionic strength, which can interfere with the electrostatic attraction between cationic peptides and anionic bacterial lipid bilayers [31][32][33]. And this is a common phenomenon for cationic peptides.…”

Section: Discussionmentioning

confidence: 99%

Selective Antifungal Activity and Fungal Biofilm Inhibition of Tryptophan Center Symmetrical Short Peptide

Chou

et al. 2021

IJMS

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Candida albicans, an opportunistic fungus, causes dental caries and contributes to mucosal bacterial dysbiosis leading to a second infection. Furthermore, C. albicans forms biofilms that are resistant to medicinal treatment. To make matters worse, antifungal resistance has spread (albeit slowly) in this species. Thus, it has been imperative to develop novel, antifungal drug compounds. Herein, a peptide was engineered with the sequence of RRFSFWFSFRR-NH2; this was named P19. This novel peptide has been observed to exert disruptive effects on fungal cell membrane physiology. Our results showed that P19 displayed high binding affinity to lipopolysaccharides (LPS), lipoteichoic acids (LTA) and the plasma membrane phosphatidylinositol (PI), phosphatidylserine (PS), cardiolipin, and phosphatidylglycerol (PG), further indicating that the molecular mechanism of P19 was not associated with the receptor recognition, but rather related to competitive interaction with the plasma membrane. In addition, compared with fluconazole and amphotericin B, P19 has been shown to have a lower potential for resistance selection than established antifungal agents.

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Section: Discussionmentioning

confidence: 99%

Selective Antifungal Activity and Fungal Biofilm Inhibition of Tryptophan Center Symmetrical Short Peptide

Chou

et al. 2021

IJMS

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“…The cytoplasmic membrane depolarization induced by the SAP was measured by the membrane potential-sensitive fluorescent dye diSC 3-5 (Sigma-Aldrich) as previously described [ 49 ]. Briefly, logarithmically growing E. coli ATCC 25922 cells were harvested by centrifugation at 1000× g for 5 min and resuspended in 5 mM HEPES buffer (pH 6.0, containing 20 mM glucose).…”

Section: Experiments Sectionmentioning

confidence: 99%

De novo design of a pH-triggered self-assembled β-hairpin nanopeptide with the dual biological functions for antibacterial and entrapment

et al. 2021

J Nanobiotechnol

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Background Acid-tolerant enteric pathogens can evade small intestinal acid barriers, colonize and infect the intestinal tract. However, broad-spectrum antibiotics are not the best therapeutic strategy because of the disruption of intestinal flora caused by its indiscriminate antimicrobial activity against beneficial and harmful bacteria. So that is what inspired us to combine pH regulation with nanotechnology to develop a pH-triggered site-targeted antimicrobial peptide with entrapping function. Results A pH-triggered dual biological functional self-assembled peptide (SAP) was designed according to the features of amino-acid building blocks and the diagonal cation–π interaction principle. The results of characterization experiments showed that changes in pH conditions could trigger microstructural transformation of the nanopeptide from nanospheres to nanofibers. The subsequent antibacterial and toxicity experiments determined that SAP had great antimicrobial activity against Escherichia coli, Salmonella typhimurium, Listeria monocytogenes, and Bacillus cereus above 15.6 μg/mL under acidic conditions by disrupting bacterial membrane integrity, excellent biocompatibility in vitro even at 250 μg/mL and high tolerance in physical environment. Moreover, at peptide concentrations greater than 62.5 μg/mL, SAP showed the entrapment property, which played an important role in phagocytic clearance in infection forces. Meanwhile, the in vivo results revealed that SAP possessed excellent therapeutic effect and good biosafety. Conclusions Our study revealed the antibacterial activity of a short β-hairpin forming self-assembled peptide, and established an innovative design strategy for peptide-based nanomaterials and a new treatment strategy for gastrointestinal bacterial infections. Graphic Abstract

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“…For example, the aggregation capability of peptides has been used as a method to increase the selectivity of peptides toward bacterial membranes, thereby causing selective toxicity in prokaryotic cells [ 5 ]. However, truncated derivatives of larger HDPs have been reported to lose antibacterial activity at smaller sizes and lower cationic charges [ 6 , 7 , 8 , 9 , 10 , 11 , 12 , 13 , 14 , 15 ]. Most of these bacterial-selective peptides engineered by fusing multiple peptide sequences are, therefore, much larger in size (>15 amino acids) and are not a cost-effective option as antimicrobial agents.…”

Section: Introductionmentioning

confidence: 99%

Bacterial-Specific Aggregation and Killing of Immunomodulatory Host Defense Peptides

2021

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This study involves the design and development of disulfide bridge-linked antimicrobial peptides using the host defense protein Angiogenin 4 (chAng4) as a template. The mini peptides derived from chAng4 (mCA4s) were evaluated for their antibacterial efficacies in various pathogenic bacterial strains, and the role of the oxidation state of thiols in the peptide sequence and its implication on antibacterial properties were explored. A remarkable property of these synthetic mCA4 peptides is their capability to flocculate bacteria and mediate bacterial-specific killing, in the absence of any other external stimulus. mCA4s were further evaluated for their cellular uptake, hemolytic activities, toxicities, and immunomodulatory activities in different eukaryotic cell lines. The results indicate that disulfide bridge-containing cationic amphipathic peptides show superior antibacterial efficacies, are nontoxic and nonhemolytic, and mediate bacterial flocculation and killing, in the absence of external stimuli.

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Binding loop of sunflower trypsin inhibitor 1 serves as a design motif for proteolysis-resistant antimicrobial peptides

Cited by 57 publications

References 56 publications

Selective Antifungal Activity and Fungal Biofilm Inhibition of Tryptophan Center Symmetrical Short Peptide

Selective Antifungal Activity and Fungal Biofilm Inhibition of Tryptophan Center Symmetrical Short Peptide

De novo design of a pH-triggered self-assembled β-hairpin nanopeptide with the dual biological functions for antibacterial and entrapment

Bacterial-Specific Aggregation and Killing of Immunomodulatory Host Defense Peptides

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