Review: Structure-Activity Relationship of Antimicrobial Peptoids
Due to their broad-spectrum activity against Gram-negative and Gram-positive bacteria, natural antimicrobial peptides (AMPs) and their synthetic analogs have emerged as prospective therapies for treating illnesses brought on by multi-drug resistant pathogens. To overcome the limitations of AMPs, suc...
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-05-01
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| Series: | Pharmaceutics |
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| Online Access: | https://www.mdpi.com/1999-4923/15/5/1506 |
| _version_ | 1797598611858522112 |
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| author | Priscilla L. Nyembe Thandokuhle Ntombela Maya M. Makatini |
| author_facet | Priscilla L. Nyembe Thandokuhle Ntombela Maya M. Makatini |
| author_sort | Priscilla L. Nyembe |
| collection | DOAJ |
| description | Due to their broad-spectrum activity against Gram-negative and Gram-positive bacteria, natural antimicrobial peptides (AMPs) and their synthetic analogs have emerged as prospective therapies for treating illnesses brought on by multi-drug resistant pathogens. To overcome the limitations of AMPs, such as protease degradation, oligo-N-substituted glycines (peptoids) are a promising alternative. Despite having the same backbone atom sequence as natural peptides, peptoid structures are more stable because, unlike AMP, their functional side chains are attached to the backbone nitrogen (N)-atom rather than the alpha carbon atom. As a result, peptoid structures are less susceptible to proteolysis and enzymatic degradation. The advantages of AMPs, such as hydrophobicity, cationic character, and amphipathicity, are mimicked by peptoids. Furthermore, structure-activity relationship studies (SAR) have shown that tuning the structure of peptoids is a crucial step in developing effective antimicrobials. |
| first_indexed | 2024-03-11T03:24:35Z |
| format | Article |
| id | doaj.art-9aa0455595ca43ce8ae147a487d80bef |
| institution | Directory Open Access Journal |
| issn | 1999-4923 |
| language | English |
| last_indexed | 2024-03-11T03:24:35Z |
| publishDate | 2023-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Pharmaceutics |
| spelling | doaj.art-9aa0455595ca43ce8ae147a487d80bef2023-11-18T02:52:34ZengMDPI AGPharmaceutics1999-49232023-05-01155150610.3390/pharmaceutics15051506Review: Structure-Activity Relationship of Antimicrobial PeptoidsPriscilla L. Nyembe0Thandokuhle Ntombela1Maya M. Makatini2Molecular Sciences Institute, School of Chemistry, University of the Witwatersrand, Johannesburg 2050, South AfricaMolecular Sciences Institute, School of Chemistry, University of the Witwatersrand, Johannesburg 2050, South AfricaMolecular Sciences Institute, School of Chemistry, University of the Witwatersrand, Johannesburg 2050, South AfricaDue to their broad-spectrum activity against Gram-negative and Gram-positive bacteria, natural antimicrobial peptides (AMPs) and their synthetic analogs have emerged as prospective therapies for treating illnesses brought on by multi-drug resistant pathogens. To overcome the limitations of AMPs, such as protease degradation, oligo-N-substituted glycines (peptoids) are a promising alternative. Despite having the same backbone atom sequence as natural peptides, peptoid structures are more stable because, unlike AMP, their functional side chains are attached to the backbone nitrogen (N)-atom rather than the alpha carbon atom. As a result, peptoid structures are less susceptible to proteolysis and enzymatic degradation. The advantages of AMPs, such as hydrophobicity, cationic character, and amphipathicity, are mimicked by peptoids. Furthermore, structure-activity relationship studies (SAR) have shown that tuning the structure of peptoids is a crucial step in developing effective antimicrobials.https://www.mdpi.com/1999-4923/15/5/1506antimicrobial peptidesantimicrobial peptoidschain lengthcationichydrophobicitycyclization |
| spellingShingle | Priscilla L. Nyembe Thandokuhle Ntombela Maya M. Makatini Review: Structure-Activity Relationship of Antimicrobial Peptoids Pharmaceutics antimicrobial peptides antimicrobial peptoids chain length cationic hydrophobicity cyclization |
| title | Review: Structure-Activity Relationship of Antimicrobial Peptoids |
| title_full | Review: Structure-Activity Relationship of Antimicrobial Peptoids |
| title_fullStr | Review: Structure-Activity Relationship of Antimicrobial Peptoids |
| title_full_unstemmed | Review: Structure-Activity Relationship of Antimicrobial Peptoids |
| title_short | Review: Structure-Activity Relationship of Antimicrobial Peptoids |
| title_sort | review structure activity relationship of antimicrobial peptoids |
| topic | antimicrobial peptides antimicrobial peptoids chain length cationic hydrophobicity cyclization |
| url | https://www.mdpi.com/1999-4923/15/5/1506 |
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