Interaction of Antimicrobial Peptide Ponericin W1, Thanatin, and Mastatopara-S with <i>Geotrichum citri-aurantii</i> Genomic DNA
Antimicrobial peptides of mastatopara-S (M-S), thanatin, and ponericin W1(P W1) were able to disrupt the membrane integrity and alter the morphology of the hyphae of <i>Geotrichum citri-aurantii</i> and then reduced the sour rot of citrus fruit. In order to understand the mechanisms of t...
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| Format: | Article |
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MDPI AG
2021-08-01
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| Series: | Foods |
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| Online Access: | https://www.mdpi.com/2304-8158/10/8/1919 |
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| author | Hongyan Zhang Sha Liu Xindan Li Wenjun Wang Lili Deng Kaifang Zeng |
| author_facet | Hongyan Zhang Sha Liu Xindan Li Wenjun Wang Lili Deng Kaifang Zeng |
| author_sort | Hongyan Zhang |
| collection | DOAJ |
| description | Antimicrobial peptides of mastatopara-S (M-S), thanatin, and ponericin W1(P W1) were able to disrupt the membrane integrity and alter the morphology of the hyphae of <i>Geotrichum citri-aurantii</i> and then reduced the sour rot of citrus fruit. In order to understand the mechanisms of thanatin, P W1 and M-S other than membrane disruption, the interaction betwixt the peptides and <i>G. citri-aurantii</i> DNA were investigated in this research. The laser confocal microscopy found that P W1, thanatin, and M-S could penetrate the cell membrane. Gel retardation assay demonstrated that P W1, thanatin, and M-S could bind to the <i>G. citri-aurantii</i> genomic DNA in vitro. UV-visible spectra and fluorescence spectra analysis further confirmed that the peptides can bind to the DNA, and then insert into the base pairs in the DNA helix, followed by wrecking the double-helix structure. In addition, M-S, thanatin, and P W1 can suppress the synthesis of DNA and RNA of <i>G. citri-aurantii</i>. |
| first_indexed | 2024-03-10T08:48:30Z |
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| id | doaj.art-250e2162eb4649c39ca24093902f26d5 |
| institution | Directory Open Access Journal |
| issn | 2304-8158 |
| language | English |
| last_indexed | 2024-03-10T08:48:30Z |
| publishDate | 2021-08-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Foods |
| spelling | doaj.art-250e2162eb4649c39ca24093902f26d52023-11-22T07:40:46ZengMDPI AGFoods2304-81582021-08-01108191910.3390/foods10081919Interaction of Antimicrobial Peptide Ponericin W1, Thanatin, and Mastatopara-S with <i>Geotrichum citri-aurantii</i> Genomic DNAHongyan Zhang0Sha Liu1Xindan Li2Wenjun Wang3Lili Deng4Kaifang Zeng5College of Food Science, Southwest University, Chongqing 400715, ChinaCollege of Food Science, Southwest University, Chongqing 400715, ChinaCollege of Food Science, Southwest University, Chongqing 400715, ChinaCollege of Food Science, Southwest University, Chongqing 400715, ChinaCollege of Food Science, Southwest University, Chongqing 400715, ChinaCollege of Food Science, Southwest University, Chongqing 400715, ChinaAntimicrobial peptides of mastatopara-S (M-S), thanatin, and ponericin W1(P W1) were able to disrupt the membrane integrity and alter the morphology of the hyphae of <i>Geotrichum citri-aurantii</i> and then reduced the sour rot of citrus fruit. In order to understand the mechanisms of thanatin, P W1 and M-S other than membrane disruption, the interaction betwixt the peptides and <i>G. citri-aurantii</i> DNA were investigated in this research. The laser confocal microscopy found that P W1, thanatin, and M-S could penetrate the cell membrane. Gel retardation assay demonstrated that P W1, thanatin, and M-S could bind to the <i>G. citri-aurantii</i> genomic DNA in vitro. UV-visible spectra and fluorescence spectra analysis further confirmed that the peptides can bind to the DNA, and then insert into the base pairs in the DNA helix, followed by wrecking the double-helix structure. In addition, M-S, thanatin, and P W1 can suppress the synthesis of DNA and RNA of <i>G. citri-aurantii</i>.https://www.mdpi.com/2304-8158/10/8/1919<i>Geotrichum citri-aurantii</i>antimicrobial peptidelocationDNA binding |
| spellingShingle | Hongyan Zhang Sha Liu Xindan Li Wenjun Wang Lili Deng Kaifang Zeng Interaction of Antimicrobial Peptide Ponericin W1, Thanatin, and Mastatopara-S with <i>Geotrichum citri-aurantii</i> Genomic DNA Foods <i>Geotrichum citri-aurantii</i> antimicrobial peptide location DNA binding |
| title | Interaction of Antimicrobial Peptide Ponericin W1, Thanatin, and Mastatopara-S with <i>Geotrichum citri-aurantii</i> Genomic DNA |
| title_full | Interaction of Antimicrobial Peptide Ponericin W1, Thanatin, and Mastatopara-S with <i>Geotrichum citri-aurantii</i> Genomic DNA |
| title_fullStr | Interaction of Antimicrobial Peptide Ponericin W1, Thanatin, and Mastatopara-S with <i>Geotrichum citri-aurantii</i> Genomic DNA |
| title_full_unstemmed | Interaction of Antimicrobial Peptide Ponericin W1, Thanatin, and Mastatopara-S with <i>Geotrichum citri-aurantii</i> Genomic DNA |
| title_short | Interaction of Antimicrobial Peptide Ponericin W1, Thanatin, and Mastatopara-S with <i>Geotrichum citri-aurantii</i> Genomic DNA |
| title_sort | interaction of antimicrobial peptide ponericin w1 thanatin and mastatopara s with i geotrichum citri aurantii i genomic dna |
| topic | <i>Geotrichum citri-aurantii</i> antimicrobial peptide location DNA binding |
| url | https://www.mdpi.com/2304-8158/10/8/1919 |
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