» Articles » PMID: 38543342

Anticancer Potential of Antimicrobial Peptides: Focus on Buforins

Overview
Publisher MDPI
Date 2024 Mar 28
PMID 38543342
Authors
Affiliations
Soon will be listed here.
Abstract

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.

Citing Articles

Encapsulated LyeTx III Peptide: Cytotoxic Agent Isolated from Spider Venom.

Santos D, Santiago L, Santos N, Romao W, Resende J, De Lima M Toxins (Basel). 2025; 17(1).

PMID: 39852985 PMC: 11768708. DOI: 10.3390/toxins17010032.


The Role and Mechanisms of Antimicrobial Peptides in Overcoming Multidrug-Resistant Bacteria.

Yang J, Zhang J, Feng Z, Ma Y Molecules. 2025; 30(1.

PMID: 39795190 PMC: 11721820. DOI: 10.3390/molecules30010128.


Enhanced Delivery and Potency of Chemotherapeutics in Melanoma Treatment via Magnetite Nanobioconjugates.

Diaz E, Quezada V, Cifuentes J, Arias Morales N, Reyes L, Munoz-Camargo C ACS Omega. 2024; 9(45):45402-45420.

PMID: 39554413 PMC: 11561594. DOI: 10.1021/acsomega.4c07415.


From defense to offense: antimicrobial peptides as promising therapeutics for cancer.

Zare-Zardini H, Saberian E, Ghanipour-Meybodi R, Jenca A, Petrasova A, Jencova J Front Oncol. 2024; 14:1463088.

PMID: 39445062 PMC: 11496142. DOI: 10.3389/fonc.2024.1463088.


Dual-Action Therapeutics: DNA Alkylation and Antimicrobial Peptides for Cancer Therapy.

Andres C, Perez de la Lastra J, Munguira E, Juan C, Perez-Lebena E Cancers (Basel). 2024; 16(18).

PMID: 39335095 PMC: 11429518. DOI: 10.3390/cancers16183123.


References
1.
Jiang Y, Chen Y, Song Z, Tan Z, Cheng J . Recent advances in design of antimicrobial peptides and polypeptides toward clinical translation. Adv Drug Deliv Rev. 2021; 170:261-280. DOI: 10.1016/j.addr.2020.12.016. View

2.
Hetz C . ER stress signaling and the BCL-2 family of proteins: from adaptation to irreversible cellular damage. Antioxid Redox Signal. 2007; 9(12):2345-55. DOI: 10.1089/ars.2007.1793. View

3.
Kobayashi S, Chikushi A, Tougu S, Imura Y, Nishida M, Yano Y . Membrane translocation mechanism of the antimicrobial peptide buforin 2. Biochemistry. 2004; 43(49):15610-6. DOI: 10.1021/bi048206q. View

4.
Anjomshoa M, Amirheidari B . Nuclease-like metalloscissors: Biomimetic candidates for cancer and bacterial and viral infections therapy. Coord Chem Rev. 2022; 458:214417. PMC: 8816526. DOI: 10.1016/j.ccr.2022.214417. View

5.
Ghanbarzadeh Z, Hemmati S, Mohagheghzadeh A . Humanizing plant-derived snakins and their encrypted antimicrobial peptides. Biochimie. 2022; 199:92-111. DOI: 10.1016/j.biochi.2022.04.011. View