How charge distribution influences the function of membrane-active peptides: Lytic or cell-penetrating?

Chen, Long; Zhang, Qiang; Yuan, Xiushuang; Cao, Yimeng; Yuan, Yanyan; Yin, Huiwei; Ding, Xin; Zhu, Zhentai; Luo, Shi-Zhong

doi:10.1016/j.biocel.2016.12.011

Cited by 25 publications

(10 citation statements)

References 16 publications

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“…membrane disruption, apoptosis induction, and internal target inhi-bition) (7,8), an initial common step in the process is their recruitment onto the bacterial cell surface (9,10). Accordingly, most AMPs display fairly conserved structural and physicochemical properties, such as positive net charge, high content of hydrophobic amino acid residues, or amphipathic structure, all favoring interaction with and insertion into membranes (11,12). Cathelicidins are a large family of AMPs whose unifying feature is the presence of a conserved cathelin (cathepsin L inhibitor) domain at the N terminus.…”

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confidence: 99%

Mechanisms of bacterial membrane permeabilization by crotalicidin (Ctn) and its fragment Ctn(15–34), antimicrobial peptides from rattlesnake venom

Pérez‐Peinado

Dias

Domingues

et al. 2018

Journal of Biological Chemistry

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Crotalicidin (Ctn), a cathelicidin-related peptide from the venom of a South American rattlesnake, possesses potent antimicrobial, antitumor, and antifungal properties. Previously, we have shown that its C-terminal fragment, Ctn(15-34), retains the antimicrobial and antitumor activities but is less toxic to healthy cells and has improved serum stability. Here, we investigated the mechanisms of action of Ctn and Ctn(15-34) against Gram-negative bacteria. Both peptides were bactericidal, killing ∼90% of and cells within 90-120 and 5-30 min, respectively. Studies of ζ potential at the bacterial cell membrane suggested that both peptides accumulate at and neutralize negative charges on the bacterial surface. Flow cytometry experiments confirmed that both peptides permeabilize the bacterial cell membrane but suggested slightly different mechanisms of action. Ctn(15-34) permeabilized the membrane immediately upon addition to the cells, whereas Ctn had a lag phase before inducing membrane damage and exhibited more complex cell-killing activity, probably because of two different modes of membrane permeabilization. Using surface plasmon resonance and leakage assays with model vesicles, we confirmed that Ctn(15-34) binds to and disrupts lipid membranes and also observed that Ctn(15-34) has a preference for vesicles that mimic bacterial or tumor cell membranes. Atomic force microscopy visualized the effect of these peptides on bacterial cells, and confocal microscopy confirmed their localization on the bacterial surface. Our studies shed light onto the antimicrobial mechanisms of Ctn and Ctn(15-34), suggesting Ctn(15-34) as a promising lead for development as an antibacterial/antitumor agent.

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confidence: 99%

Mechanisms of bacterial membrane permeabilization by crotalicidin (Ctn) and its fragment Ctn(15–34), antimicrobial peptides from rattlesnake venom

Pérez‐Peinado

Dias

Domingues

et al. 2018

Journal of Biological Chemistry

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“…Hallbrink et al reported that while a higher hydrophobic moment increased cell penetration, it also caused increased membrane leakage as a result of irreversible pore formation [33]. Chen et al also reported that amphipathic peptides with a concentrated charge distribution caused lysis in HeLa cells, while peptides with disperse charge distribution did not exhibit lytic activity [34]. The distribution of the cationic arginine residues is more concentrated in Pep2 than that of RALA, which is equipped with many spacer alanine residues.…”

Section: Discussionmentioning

confidence: 99%

Rational design and characterisation of an amphipathic cell penetrating peptide for non-viral gene delivery

McErlean

McCrudden

McBride

et al. 2021

International Journal of Pharmaceutics

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“…The exact mechanism by which AMPs exert their bactericidal activity has not been fully elucidated. However, because bacterial membranes are rich in anionic lipids such as phosphatidylserine and cardiolipin, it is generally believed that positively charged peptides interact with negatively charged bacterial cell membranes, resulting in increased membrane permeability and rapid cell death (Chen et al 2017). The mode of action of AMPs depends on their properties, such as their sequence, size, charge, hydrophobicity, and affinity (Bhattacharjya et al 2009).…”

Section: Mechanisms Of Plant Amp Activitiesmentioning

confidence: 99%

Plant antimicrobial peptides: structures, functions, and applications

Jian

et al. 2021

Bot Stud

125

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Antimicrobial peptides (AMPs) are a class of short, usually positively charged polypeptides that exist in humans, animals, and plants. Considering the increasing number of drug-resistant pathogens, the antimicrobial activity of AMPs has attracted much attention. AMPs with broad-spectrum antimicrobial activity against many gram-positive bacteria, gram-negative bacteria, and fungi are an important defensive barrier against pathogens for many organisms. With continuing research, many other physiological functions of plant AMPs have been found in addition to their antimicrobial roles, such as regulating plant growth and development and treating many diseases with high efficacy. The potential applicability of plant AMPs in agricultural production, as food additives and disease treatments, has garnered much interest. This review focuses on the types of plant AMPs, their mechanisms of action, the parameters affecting the antimicrobial activities of AMPs, and their potential applications in agricultural production, the food industry, breeding industry, and medical field.

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How charge distribution influences the function of membrane-active peptides: Lytic or cell-penetrating?

Cited by 25 publications

References 16 publications

Mechanisms of bacterial membrane permeabilization by crotalicidin (Ctn) and its fragment Ctn(15–34), antimicrobial peptides from rattlesnake venom

Mechanisms of bacterial membrane permeabilization by crotalicidin (Ctn) and its fragment Ctn(15–34), antimicrobial peptides from rattlesnake venom

Rational design and characterisation of an amphipathic cell penetrating peptide for non-viral gene delivery

Plant antimicrobial peptides: structures, functions, and applications

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