Multiple strategies of HSP antimicrobial peptide optimization to enhance antimicrobial activity
Abstract Antimicrobial peptides (AMPs) have caught the attention of researchers over the last couple of years due to their unique membrane lytic mechanism for combating antibiotic resistance, which differs from the molecular targets of traditional antibiotics. Although natural AMPs exhibit potential...
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| Format: | Article |
| Language: | English |
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Springer
2024-11-01
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| Series: | Amino Acids |
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| Online Access: | https://doi.org/10.1007/s00726-024-03428-z |
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| author | Xiaozhong Cheng Yonghuang Zhang Yan Zhang Yajun Chen Jianli Chen Wei Wang Guilan Zhu |
| author_facet | Xiaozhong Cheng Yonghuang Zhang Yan Zhang Yajun Chen Jianli Chen Wei Wang Guilan Zhu |
| author_sort | Xiaozhong Cheng |
| collection | DOAJ |
| description | Abstract Antimicrobial peptides (AMPs) have caught the attention of researchers over the last couple of years due to their unique membrane lytic mechanism for combating antibiotic resistance, which differs from the molecular targets of traditional antibiotics. Although natural AMPs exhibit potential antimicrobial activity against a wide range of microorganisms, some drawbacks, such as toxicity, low antibacterial activity, and high production costs limit their clinical application. To enhance the antimicrobial activity of a series of HSP peptides derived from the natural peptide HSP-1, this study optimized them using a variety of strategies, including net charge, hydrophobic moment, hydrophobicity, and helicity. Optimizing the antimicrobial action of HSP peptides depended mostly on net charge, hydrophobic moment, and hydrophobicity rather than helicity. HSP-M4 may be designed to combat microbial infections because the antimicrobial activity and cytotoxicity assays showed that they exhibited low cytotoxicity and prominent antimicrobial activity, respectively. |
| format | Article |
| id | doaj-art-bb7dd88b83c04100b01ae6006e402a95 |
| institution | Kabale University |
| issn | 1438-2199 |
| language | English |
| publishDate | 2024-11-01 |
| publisher | Springer |
| record_format | Article |
| series | Amino Acids |
| spelling | doaj-art-bb7dd88b83c04100b01ae6006e402a952024-12-22T12:34:40ZengSpringerAmino Acids1438-21992024-11-0156111010.1007/s00726-024-03428-zMultiple strategies of HSP antimicrobial peptide optimization to enhance antimicrobial activityXiaozhong Cheng0Yonghuang Zhang1Yan Zhang2Yajun Chen3Jianli Chen4Wei Wang5Guilan Zhu6Anhui Province Green Food Collaborative Technology Service Center for Rural Revitalization, Hefei Normal UniversityDepartment of Pharmacy, Hefei Binhu HospitalAnhui Province Green Food Collaborative Technology Service Center for Rural Revitalization, Hefei Normal UniversityAnhui Province Green Food Collaborative Technology Service Center for Rural Revitalization, Hefei Normal UniversityShimadzu (China) Co., LtdAnhui Province Green Food Collaborative Technology Service Center for Rural Revitalization, Hefei Normal UniversityAnhui Province Green Food Collaborative Technology Service Center for Rural Revitalization, Hefei Normal UniversityAbstract Antimicrobial peptides (AMPs) have caught the attention of researchers over the last couple of years due to their unique membrane lytic mechanism for combating antibiotic resistance, which differs from the molecular targets of traditional antibiotics. Although natural AMPs exhibit potential antimicrobial activity against a wide range of microorganisms, some drawbacks, such as toxicity, low antibacterial activity, and high production costs limit their clinical application. To enhance the antimicrobial activity of a series of HSP peptides derived from the natural peptide HSP-1, this study optimized them using a variety of strategies, including net charge, hydrophobic moment, hydrophobicity, and helicity. Optimizing the antimicrobial action of HSP peptides depended mostly on net charge, hydrophobic moment, and hydrophobicity rather than helicity. HSP-M4 may be designed to combat microbial infections because the antimicrobial activity and cytotoxicity assays showed that they exhibited low cytotoxicity and prominent antimicrobial activity, respectively.https://doi.org/10.1007/s00726-024-03428-zAntimicrobial peptidesHSP-1Antimicrobial activityOptimization |
| spellingShingle | Xiaozhong Cheng Yonghuang Zhang Yan Zhang Yajun Chen Jianli Chen Wei Wang Guilan Zhu Multiple strategies of HSP antimicrobial peptide optimization to enhance antimicrobial activity Amino Acids Antimicrobial peptides HSP-1 Antimicrobial activity Optimization |
| title | Multiple strategies of HSP antimicrobial peptide optimization to enhance antimicrobial activity |
| title_full | Multiple strategies of HSP antimicrobial peptide optimization to enhance antimicrobial activity |
| title_fullStr | Multiple strategies of HSP antimicrobial peptide optimization to enhance antimicrobial activity |
| title_full_unstemmed | Multiple strategies of HSP antimicrobial peptide optimization to enhance antimicrobial activity |
| title_short | Multiple strategies of HSP antimicrobial peptide optimization to enhance antimicrobial activity |
| title_sort | multiple strategies of hsp antimicrobial peptide optimization to enhance antimicrobial activity |
| topic | Antimicrobial peptides HSP-1 Antimicrobial activity Optimization |
| url | https://doi.org/10.1007/s00726-024-03428-z |
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