The Antimicrobial Peptide Melectin Shows Both Antimicrobial and Antitumor Activity via Membrane Interference and DNA Binding
Purpose: Increasingly complex diseases require novel drugs for their treatment. Antimicrobial peptides (AMPs) are promising candidate treatments due to their broad existence and special characteristics. However, the current understanding of AMPs is not sufficient to allow them to be produced commerc...
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| Veröffentlicht in: | Drug design, development and therapy development and therapy, 2021-01, Vol.15, p.1261-1273 |
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| creator | Liang, Xiaolei Yan, Jiexi Lu, Yingwei Liu, Shan Chai, Xiaojing |
| description | Purpose: Increasingly complex diseases require novel drugs for their treatment. Antimicrobial peptides (AMPs) are promising candidate treatments due to their broad existence and special characteristics. However, the current understanding of AMPs is not sufficient to allow them to be produced commercially for clinical use.
Materials and Methods: Melectin, from the venom of the cleptoparasitic bee Melecta albifrons, does not exhibit sequence homology with other wasp venom peptides. To investigate this more deeply, we explored the antibacterial and antitumor activities of Melectin and related mechanisms.
Results: Our results demonstrate that Melectin possesses antimicrobial properties against standard sensitive/clinical drug-resistant bacteria strains as well as antitumor activity. It has an a-helix form and exhibits moderate cytotoxicity. Its action mechanisms are involved with membrane interfering and DNA binding. The membrane interfering effect was distinct between different phospholipid compositions.
Conclusion: We found that Melectin may serve as a new potential template in the battle against multidrug resistance, and our study indicated that there are promising prospects for medically applicable drugs based on AMPs. |
| doi_str_mv | 10.2147/DDDT.S288219 |
| format | Article |
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Materials and Methods: Melectin, from the venom of the cleptoparasitic bee Melecta albifrons, does not exhibit sequence homology with other wasp venom peptides. To investigate this more deeply, we explored the antibacterial and antitumor activities of Melectin and related mechanisms.
Results: Our results demonstrate that Melectin possesses antimicrobial properties against standard sensitive/clinical drug-resistant bacteria strains as well as antitumor activity. It has an a-helix form and exhibits moderate cytotoxicity. Its action mechanisms are involved with membrane interfering and DNA binding. The membrane interfering effect was distinct between different phospholipid compositions.
Conclusion: We found that Melectin may serve as a new potential template in the battle against multidrug resistance, and our study indicated that there are promising prospects for medically applicable drugs based on AMPs.</description><identifier>ISSN: 1177-8881</identifier><identifier>EISSN: 1177-8881</identifier><identifier>DOI: 10.2147/DDDT.S288219</identifier><identifier>PMID: 33776423</identifier><language>eng</language><publisher>ALBANY: Dove Medical Press Ltd</publisher><subject>action mechanism ; Animals ; Anti-Bacterial Agents - chemistry ; Anti-Bacterial Agents - pharmacology ; antibacterial ; Anticancer properties ; Antimicrobial agents ; Antimicrobial Cationic Peptides - chemistry ; Antimicrobial Cationic Peptides - pharmacology ; antimicrobial peptide ; Antimicrobial peptides ; Antineoplastic Agents - chemistry ; Antineoplastic Agents - pharmacology ; antitumor ; Antitumor activity ; Bacteria ; Binding ; Binding Sites - drug effects ; Cell Line ; Cell Proliferation - drug effects ; Chemistry, Medicinal ; Cytotoxicity ; Deoxyribonucleic acid ; DNA ; DNA - drug effects ; DNA-ligand interactions ; Drug development ; Drug resistance ; Drug resistance in microorganisms ; Drug Resistance, Bacterial - drug effects ; Drug Screening Assays, Antitumor ; E coli ; Escherichia coli - drug effects ; Ethylenediaminetetraacetic acid ; Homology ; Humans ; Kinetics ; Life Sciences & Biomedicine ; Medical research ; Medical treatment ; melectin ; Membranes ; Mice ; Microbial Sensitivity Tests ; Multidrug resistance ; Original Research ; Peptides ; Permeability ; Pharmacology & Pharmacy ; Phospholipids ; Plasmids ; Quality of life ; Science & Technology ; Toxicity ; Venom ; Wasps</subject><ispartof>Drug design, development and therapy, 2021-01, Vol.15, p.1261-1273</ispartof><rights>2021 Liang et al.</rights><rights>COPYRIGHT 2021 Dove Medical Press Limited</rights><rights>2021. This work is licensed under https://creativecommons.org/licenses/by-nc/3.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2021 Liang et al. 2021 Liang et al.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>true</woscitedreferencessubscribed><woscitedreferencescount>5</woscitedreferencescount><woscitedreferencesoriginalsourcerecordid>wos000632961200001</woscitedreferencesoriginalsourcerecordid><citedby>FETCH-LOGICAL-c619t-980c27bbdec36026ef6a852f6a1b9c8c50d6f785905ef87936b8a597c226394e3</citedby><cites>FETCH-LOGICAL-c619t-980c27bbdec36026ef6a852f6a1b9c8c50d6f785905ef87936b8a597c226394e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7989573/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7989573/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,728,781,785,865,886,2103,2115,3863,27929,27930,39263,53796,53798</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33776423$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Liang, Xiaolei</creatorcontrib><creatorcontrib>Yan, Jiexi</creatorcontrib><creatorcontrib>Lu, Yingwei</creatorcontrib><creatorcontrib>Liu, Shan</creatorcontrib><creatorcontrib>Chai, Xiaojing</creatorcontrib><title>The Antimicrobial Peptide Melectin Shows Both Antimicrobial and Antitumor Activity via Membrane Interference and DNA Binding</title><title>Drug design, development and therapy</title><addtitle>DRUG DES DEV THER</addtitle><addtitle>Drug Des Devel Ther</addtitle><description>Purpose: Increasingly complex diseases require novel drugs for their treatment. Antimicrobial peptides (AMPs) are promising candidate treatments due to their broad existence and special characteristics. However, the current understanding of AMPs is not sufficient to allow them to be produced commercially for clinical use.
Materials and Methods: Melectin, from the venom of the cleptoparasitic bee Melecta albifrons, does not exhibit sequence homology with other wasp venom peptides. To investigate this more deeply, we explored the antibacterial and antitumor activities of Melectin and related mechanisms.
Results: Our results demonstrate that Melectin possesses antimicrobial properties against standard sensitive/clinical drug-resistant bacteria strains as well as antitumor activity. It has an a-helix form and exhibits moderate cytotoxicity. Its action mechanisms are involved with membrane interfering and DNA binding. The membrane interfering effect was distinct between different phospholipid compositions.
Conclusion: We found that Melectin may serve as a new potential template in the battle against multidrug resistance, and our study indicated that there are promising prospects for medically applicable drugs based on AMPs.</description><subject>action mechanism</subject><subject>Animals</subject><subject>Anti-Bacterial Agents - chemistry</subject><subject>Anti-Bacterial Agents - pharmacology</subject><subject>antibacterial</subject><subject>Anticancer properties</subject><subject>Antimicrobial agents</subject><subject>Antimicrobial Cationic Peptides - chemistry</subject><subject>Antimicrobial Cationic Peptides - pharmacology</subject><subject>antimicrobial peptide</subject><subject>Antimicrobial peptides</subject><subject>Antineoplastic Agents - chemistry</subject><subject>Antineoplastic Agents - pharmacology</subject><subject>antitumor</subject><subject>Antitumor activity</subject><subject>Bacteria</subject><subject>Binding</subject><subject>Binding Sites - drug effects</subject><subject>Cell Line</subject><subject>Cell Proliferation - drug effects</subject><subject>Chemistry, Medicinal</subject><subject>Cytotoxicity</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA - drug effects</subject><subject>DNA-ligand interactions</subject><subject>Drug development</subject><subject>Drug resistance</subject><subject>Drug resistance in microorganisms</subject><subject>Drug Resistance, Bacterial - drug effects</subject><subject>Drug Screening Assays, Antitumor</subject><subject>E coli</subject><subject>Escherichia coli - drug effects</subject><subject>Ethylenediaminetetraacetic acid</subject><subject>Homology</subject><subject>Humans</subject><subject>Kinetics</subject><subject>Life Sciences & Biomedicine</subject><subject>Medical research</subject><subject>Medical treatment</subject><subject>melectin</subject><subject>Membranes</subject><subject>Mice</subject><subject>Microbial Sensitivity Tests</subject><subject>Multidrug resistance</subject><subject>Original Research</subject><subject>Peptides</subject><subject>Permeability</subject><subject>Pharmacology & Pharmacy</subject><subject>Phospholipids</subject><subject>Plasmids</subject><subject>Quality of life</subject><subject>Science & Technology</subject><subject>Toxicity</subject><subject>Venom</subject><subject>Wasps</subject><issn>1177-8881</issn><issn>1177-8881</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>HGBXW</sourceid><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><sourceid>DOA</sourceid><recordid>eNqNkttr2zAYxc3YWLtub3sehsEYbMl0iWXpZZAmuwS6CzR7FrL0OVFwpEyWWwr74ycnWZaUPQyDLT7_zpF8fLLsOUZDgkflu-l0Oh9eE84JFg-yc4zLcsA5xw-P1mfZk7ZdIcQoI-hxdkZpWbIRoefZr_kS8rGLdm118JVVTf4dNtEayL9AAzpal18v_W2bX_q4vEcqZ7aT2K19yMcJvrHxLr-xKonXVVAO8pmLEGoI4DRsBdOv4_zSOmPd4mn2qFZNC8_2z4vsx8cP88nnwdW3T7PJ-GqgGRZxIDjSpKwqA5oyRBjUTPGCpDuuhOa6QIbVJS8EKqDmpaCs4qoQpSaEUTECepHNdr7Gq5XcBLtW4U56ZeV24MNCqhCtbkBigWjNgaGa45HRplKGUGoqM0KoTpsnr_c7r01XrcFocDGo5sT09I2zS7nwN7IUXBQlTQav9wbB_-ygjXJtWw1Nk9LyXStJgViBCaE8oS_voSvfBZeiShSmrBiViP6lFip9gHW1T_vq3lSOWQqFEEF7avgPKl0G0g_1Dmqb5ieCV0eCJagmLlvfdNF6156Cb3dgqkXbBqgPYWAk-4rKvqJyX9GEvzgO8AD_6WQC-A64hcrXrbZ9dQ4Y6ltMBMMkrRCe2Kj6E01852KSvvl_Kf0N_T8AUw</recordid><startdate>20210101</startdate><enddate>20210101</enddate><creator>Liang, Xiaolei</creator><creator>Yan, Jiexi</creator><creator>Lu, Yingwei</creator><creator>Liu, Shan</creator><creator>Chai, Xiaojing</creator><general>Dove Medical Press Ltd</general><general>Dove Medical Press Limited</general><general>Taylor & Francis Ltd</general><general>Dove</general><general>Dove Medical Press</general><scope>BLEPL</scope><scope>DTL</scope><scope>HGBXW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QO</scope><scope>7RV</scope><scope>7XB</scope><scope>8FD</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>KB0</scope><scope>M2O</scope><scope>MBDVC</scope><scope>NAPCQ</scope><scope>P64</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20210101</creationdate><title>The Antimicrobial Peptide Melectin Shows Both Antimicrobial and Antitumor Activity via Membrane Interference and DNA Binding</title><author>Liang, Xiaolei ; Yan, Jiexi ; Lu, Yingwei ; Liu, Shan ; Chai, Xiaojing</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c619t-980c27bbdec36026ef6a852f6a1b9c8c50d6f785905ef87936b8a597c226394e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>action mechanism</topic><topic>Animals</topic><topic>Anti-Bacterial Agents - chemistry</topic><topic>Anti-Bacterial Agents - pharmacology</topic><topic>antibacterial</topic><topic>Anticancer properties</topic><topic>Antimicrobial agents</topic><topic>Antimicrobial Cationic Peptides - chemistry</topic><topic>Antimicrobial Cationic Peptides - pharmacology</topic><topic>antimicrobial peptide</topic><topic>Antimicrobial peptides</topic><topic>Antineoplastic Agents - chemistry</topic><topic>Antineoplastic Agents - pharmacology</topic><topic>antitumor</topic><topic>Antitumor activity</topic><topic>Bacteria</topic><topic>Binding</topic><topic>Binding Sites - drug effects</topic><topic>Cell Line</topic><topic>Cell Proliferation - drug effects</topic><topic>Chemistry, Medicinal</topic><topic>Cytotoxicity</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>DNA - drug effects</topic><topic>DNA-ligand interactions</topic><topic>Drug development</topic><topic>Drug resistance</topic><topic>Drug resistance in microorganisms</topic><topic>Drug Resistance, Bacterial - drug effects</topic><topic>Drug Screening Assays, Antitumor</topic><topic>E coli</topic><topic>Escherichia coli - drug effects</topic><topic>Ethylenediaminetetraacetic acid</topic><topic>Homology</topic><topic>Humans</topic><topic>Kinetics</topic><topic>Life Sciences & Biomedicine</topic><topic>Medical research</topic><topic>Medical treatment</topic><topic>melectin</topic><topic>Membranes</topic><topic>Mice</topic><topic>Microbial Sensitivity Tests</topic><topic>Multidrug resistance</topic><topic>Original Research</topic><topic>Peptides</topic><topic>Permeability</topic><topic>Pharmacology & Pharmacy</topic><topic>Phospholipids</topic><topic>Plasmids</topic><topic>Quality of life</topic><topic>Science & Technology</topic><topic>Toxicity</topic><topic>Venom</topic><topic>Wasps</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Liang, Xiaolei</creatorcontrib><creatorcontrib>Yan, Jiexi</creatorcontrib><creatorcontrib>Lu, Yingwei</creatorcontrib><creatorcontrib>Liu, Shan</creatorcontrib><creatorcontrib>Chai, Xiaojing</creatorcontrib><collection>Web of Science Core Collection</collection><collection>Science Citation Index Expanded</collection><collection>Web of Science - Science Citation Index Expanded - 2021</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Biotechnology Research Abstracts</collection><collection>Nursing & Allied Health Database</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Technology Research Database</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Research Library</collection><collection>Research Library (Corporate)</collection><collection>Nursing & Allied Health Premium</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Access via ProQuest (Open Access)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>Drug design, development and therapy</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Liang, Xiaolei</au><au>Yan, Jiexi</au><au>Lu, Yingwei</au><au>Liu, Shan</au><au>Chai, Xiaojing</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Antimicrobial Peptide Melectin Shows Both Antimicrobial and Antitumor Activity via Membrane Interference and DNA Binding</atitle><jtitle>Drug design, development and therapy</jtitle><stitle>DRUG DES DEV THER</stitle><addtitle>Drug Des Devel Ther</addtitle><date>2021-01-01</date><risdate>2021</risdate><volume>15</volume><spage>1261</spage><epage>1273</epage><pages>1261-1273</pages><issn>1177-8881</issn><eissn>1177-8881</eissn><abstract>Purpose: Increasingly complex diseases require novel drugs for their treatment. Antimicrobial peptides (AMPs) are promising candidate treatments due to their broad existence and special characteristics. However, the current understanding of AMPs is not sufficient to allow them to be produced commercially for clinical use.
Materials and Methods: Melectin, from the venom of the cleptoparasitic bee Melecta albifrons, does not exhibit sequence homology with other wasp venom peptides. To investigate this more deeply, we explored the antibacterial and antitumor activities of Melectin and related mechanisms.
Results: Our results demonstrate that Melectin possesses antimicrobial properties against standard sensitive/clinical drug-resistant bacteria strains as well as antitumor activity. It has an a-helix form and exhibits moderate cytotoxicity. Its action mechanisms are involved with membrane interfering and DNA binding. The membrane interfering effect was distinct between different phospholipid compositions.
Conclusion: We found that Melectin may serve as a new potential template in the battle against multidrug resistance, and our study indicated that there are promising prospects for medically applicable drugs based on AMPs.</abstract><cop>ALBANY</cop><pub>Dove Medical Press Ltd</pub><pmid>33776423</pmid><doi>10.2147/DDDT.S288219</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | action mechanism Animals Anti-Bacterial Agents - chemistry Anti-Bacterial Agents - pharmacology antibacterial Anticancer properties Antimicrobial agents Antimicrobial Cationic Peptides - chemistry Antimicrobial Cationic Peptides - pharmacology antimicrobial peptide Antimicrobial peptides Antineoplastic Agents - chemistry Antineoplastic Agents - pharmacology antitumor Antitumor activity Bacteria Binding Binding Sites - drug effects Cell Line Cell Proliferation - drug effects Chemistry, Medicinal Cytotoxicity Deoxyribonucleic acid DNA DNA - drug effects DNA-ligand interactions Drug development Drug resistance Drug resistance in microorganisms Drug Resistance, Bacterial - drug effects Drug Screening Assays, Antitumor E coli Escherichia coli - drug effects Ethylenediaminetetraacetic acid Homology Humans Kinetics Life Sciences & Biomedicine Medical research Medical treatment melectin Membranes Mice Microbial Sensitivity Tests Multidrug resistance Original Research Peptides Permeability Pharmacology & Pharmacy Phospholipids Plasmids Quality of life Science & Technology Toxicity Venom Wasps |
| title | The Antimicrobial Peptide Melectin Shows Both Antimicrobial and Antitumor Activity via Membrane Interference and DNA Binding |
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