Antimicrobial activity of histone1-derived peptides from large yellow croaker Larimichthys crocea

Ma, Xiaowan; Jin, Yuan; Qiao, Ying; Zhong, Shaobin; Xing, Yongze; Chen, Xuyang

doi:10.1016/j.aquaculture.2023.739430

Cited by 4 publications

(1 citation statement)

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“…The molecular process of membrane penetration and the disruption of AMPs depends on various variables, such as the sequence of amino acids in the membrane, the amount of peptides, and the lipids in the membrane [ 39 ]. Almost all AMPs tend to be classified into two mechanistic pathways depending on their cell membrane interaction [ 61 , 62 , 63 , 64 ]. The first category focuses on cell wall disruption peptides that can distinguish between bacterial and human or host cells [ 43 , 65 , 66 , 67 ], and their cell wall penetrative properties include the following models: carpet, staves of a barrel, micellar aggregate, and toroidal pores (e.g., magainin-2, protegrin-1) [ 39 , 67 ].…”

Section: Antimicrobial Peptides (Amps) With Anticancer Potentialmentioning

confidence: 99%

Anticancer Potential of Antimicrobial Peptides: Focus on Buforins

Tolos (Vasii),

Moisa,

Dochia

et al. 2024

Polymers

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In seeking alternative cancer treatments, antimicrobial peptides (AMPs), sourced from various life forms, emerge as promising contenders. These endogenous peptides, also known as host defense peptides (HDPs), play crucial roles in immune defenses against infections and exhibit potential in combating cancers. With their diverse defensive functions, plant-derived AMPs, such as thionins and defensins, offer a rich repertoire of antimicrobial properties. Insects, amphibians, and animals contribute unique AMPs like cecropins, temporins, and cathelicidins, showcasing broad-spectrum activities against bacteria, fungi, and viruses. Understanding these natural peptides holds significant potential for developing effective and targeted therapies against cancer and infectious diseases. Antimicrobial peptides (AMPs) exhibit diverse structural characteristics, including α-helical, β-sheet, extended, and loop peptides. Environmental conditions influence their structure, connecting to changes in cell membrane hydrophobicity. AMPs’ actions involve direct killing and immune regulation, with additional activities like membrane depolarization. In this review, we focus on antimicrobial peptides that act as anticancer agents and AMPs that exhibit mechanisms akin to antimicrobial activity. Buforin AMPs, particularly Buforin I and II, derived from histone H2A, demonstrate antibacterial and anticancer potential. Buforin IIb and its analogs show promise, with selectivity for cancer cells. Despite the challenges, AMPs offer a unique approach to combat microbial resistance and potential cancer treatment. In various cancer types, including HeLa, breast, lung, ovarian, prostate, and liver cancers, buforins demonstrate inhibitory effects and apoptosis induction. To address limitations like stability and bioavailability, researchers explore buforin-containing bioconjugates, covalently linked with nanoparticles or liposomes. Bioconjugation enhances specificity-controlled release and combats drug resistance, presenting a promising avenue for targeted cancer treatment. Clinical translation awaits further evaluation through in vivo studies and future clinical trials.

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