Hydrophilic Linear Peptide with Histidine and Lysine Residues as a Key Factor Affecting Antifungal Activity

Park, Seong-Cheol; Kim, Jin‐Young; Kim, Young Ho; Cheong, Gang-Won; Lee, Yong Jae; Choi, Wonkyun; Lee, Jung Ro; Jang, Mi-Kyeong

doi:10.3390/ijms19123781

Cited by 14 publications

(7 citation statements)

References 39 publications

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“…The diversity of synthetic peptides entering clinical trials has increased over the last 13 years, stimulating advances in Fmoc SPPS technologies in response to the growing demand for medicinal chemistry and pharmacology (Behrendt et al, 2016). Several groups have synthesized linear (Tran et al, 2008;Magliani et al, 2011;Konno et al, 2015;Cools et al, 2017;Park et al, 2018) and cyclic peptides (Mosca et al, 2000;Schaaper et al, 2001;Konno et al, 2015;Ng-Choi et al, 2019) using Fmoc SPPS.…”

Section: Chemical Synthesismentioning

confidence: 99%

Antifungal Peptides as Therapeutic Agents

Ullivarri

Arbulu

García-Gutiérrez

et al. 2020

Front. Cell. Infect. Microbiol.

160

132

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Fungi have been used since ancient times in food and beverage-making processes and, more recently, have been harnessed for the production of antibiotics and in processes of relevance to the bioeconomy. Moreover, they are starting to gain attention as a key component of the human microbiome. However, fungi are also responsible for human infections. The incidence of community-acquired and nosocomial fungal infections has increased considerably in recent decades. Antibiotic resistance development, the increasing number of immunodeficiency-and/or immunosuppression-related diseases and limited therapeutic options available are triggering the search for novel alternatives. These new antifungals should be less toxic for the host, with targeted or broader antimicrobial spectra (for diseases of known and unknown etiology, respectively) and modes of actions that limit the potential for the emergence of resistance among pathogenic fungi. Given these criteria, antimicrobial peptides with antifungal properties, i.e., antifungal peptides (AFPs), have emerged as powerful candidates due to their efficacy and high selectivity. In this review, we provide an overview of the bioactivity and classification of AFPs (natural and synthetic) as well as their mode of action and advantages over current antifungal drugs. Additionally, natural, heterologous and synthetic production of AFPs with a view to greater levels of exploitation is discussed. Finally, we evaluate the current and potential applications of these peptides, along with the future challenges relating to antifungal treatments.

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Section: Chemical Synthesismentioning

confidence: 99%

Antifungal Peptides as Therapeutic Agents

Ullivarri

Arbulu

García-Gutiérrez

et al. 2020

Front. Cell. Infect. Microbiol.

160

132

View full text Add to dashboard Cite

show abstract

“…Antifungal peptides are produced by several organisms, including insects, plants, fungi, and bacteria ( Maskey et al, 2003 ; Wen et al, 2014 ; Al Souhail et al, 2016 ; Khani et al, 2019 ). Most antifungal peptides are composed of 10–100 amino acid residues, and are classified as lipopeptides and linear, cyclic, and glucan peptides ( Donzelli et al, 2001 ; Ortiz-Lopez et al, 2015 ; Park et al, 2018 ). Several mechanisms through which antifungal peptides inhibit fungal growth have been elucidated, which include the blocking of the biosynthesis of chitin and b-glucan, two major fungal cell wall components ( Donzelli et al, 2001 ; Pushpanathan et al, 2012 ; Moghaddam et al, 2017 ; Tong et al, 2020 ).…”

Section: Discussionmentioning

confidence: 99%

His-Ala-Phe-Lys peptide from Burkholderia arboris possesses antifungal activity

Zhu

Chen

et al. 2022

Front. Microbiol.

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Burkholderia arboris, which belongs to the Burkholderia cepacia complex, has been shown to possess antifungal activity against several plant fungal pathogens; however, the antifungal compounds are yet to be identified. Here, we identified the antifungal compounds produced by B. arboris using genetic and metabolomic approaches. We generated a Tn5 transposon mutation library of 3,000 B. arboris mutants and isolated three mutants with reduced antifungal activity against the plant fungal pathogen Fusarium oxysporum. Among the mutants, the M464 mutant exhibited the weakest antifungal activity. In the M464 genome, the transposon was inserted into the cobA gene, encoding uroporphyrin-III methyltransferase. Deletion of the cobA gene also resulted in reduced antifungal activity, indicating that the cobA gene contributed to the antifungal activity of B. arboris. Furthermore, a comparison of the differential metabolites between wild type B. arboris and the ∆cobA mutant showed a significantly decreased level of tetrapeptide His-Ala-Phe-Lys (Hafk) in the ∆cobA mutant. Therefore, a Hafk peptide with D-amino acid residues was synthesized and its antifungal activity was evaluated. Notably, the Hafk peptide displayed significant antifungal activity against F. oxysporum and Botrytis cinerea, two plant pathogens that cause destructive fungal diseases. Overall, a novel antifungal compound (Hafk) that can be used for the biocontrol of fungal diseases in plants was identified in B. arboris.

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“…albicans (Korea Collection for Type Culture [KCTC] 7270) was used as a reference strain, and it was isolated from a human skin lesion of erosion interdigitalis in Uruguay and purchased from the KCTC. C. albicans (Culture Collection of Antibiotics Resistant Microbes [CCARM] 14001, CCARM 14004, and CCARM 14007) isolated in 1999, as well as C. albicans (CCARM 14020) isolated in 2002, were used as representative drug-resistant strains and were purchased from the CCARM [17]. S. aureus (American Type Culture Collection [ATCC] 25923) was purchased from the ATCC.…”

Section: Methodsmentioning

confidence: 99%

Lycosin-II Exhibits Antifungal Activity and Inhibits Dual-Species Biofilm by Candida albicans and Staphylococcus aureus

Park

Kim

Kang

et al. 2022

JoF

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The increase and dissemination of antimicrobial resistance is a global public health issue. To address this, new antimicrobial agents have been developed. Antimicrobial peptides (AMPs) exhibit a wide range of antimicrobial activities against pathogens, including bacteria and fungi. Lycosin-II, isolated from the venom of the spider Lycosa singoriensis, has shown antibacterial activity by disrupting membranes. However, the mode of action of Lycosin-II and its antifungal activity have not been clearly described. Therefore, we confirmed that Lycosin-II showed antifungal activity against Candida albicans (C. albicans). To investigate the mode of action, membrane-related assays were performed, including an evaluation of C. albicans membrane depolarization and membrane integrity after exposure to Lycosin-II. Our results indicated that Lycosin-II damaged the C. albicans membrane. Additionally, Lycosin-II induced oxidative stress through the generation of reactive oxygen species (ROS) in C. albicans. Moreover, Lycosin-II exhibited an inhibitory effect on dual-species biofilm formation by C. albicans and Staphylococcus aureus (S. aureus), which are the most co-isolated fungi and bacteria. These results revealed that Lycosin-II can be utilized against C. albicans and dual-species strain infections.

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Hydrophilic Linear Peptide with Histidine and Lysine Residues as a Key Factor Affecting Antifungal Activity

Cited by 14 publications

References 39 publications

Antifungal Peptides as Therapeutic Agents

Antifungal Peptides as Therapeutic Agents

His-Ala-Phe-Lys peptide from Burkholderia arboris possesses antifungal activity

Lycosin-II Exhibits Antifungal Activity and Inhibits Dual-Species Biofilm by Candida albicans and Staphylococcus aureus

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