NMR assisted studies on the solution structures and functions of antimicrobial peptides
Microbial resistance has now become a global public health concern, and the spread of multidrug-resistant bacteria also threatens human health. Antimicrobial peptides (AMPs) are a class of small peptides with antibacterial, anti-inflammatory, anti-infective, anti-oxidation, anti-tumor, antiviral fun...
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| Format: | Article |
| Language: | English |
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KeAi Communications Co. Ltd.
2022-11-01
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| Series: | Magnetic Resonance Letters |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2772516222000390 |
| _version_ | 1828115873116717056 |
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| author | Yaying Zhang Chunyang Cao |
| author_facet | Yaying Zhang Chunyang Cao |
| author_sort | Yaying Zhang |
| collection | DOAJ |
| description | Microbial resistance has now become a global public health concern, and the spread of multidrug-resistant bacteria also threatens human health. Antimicrobial peptides (AMPs) are a class of small peptides with antibacterial, anti-inflammatory, anti-infective, anti-oxidation, anti-tumor, antiviral functions and immune regulation activities. Due to the small sizes, their structures are easily studied by nuclear magnetic resonance (NMR) techniques. Compared to traditional antibiotics, AMPs have specific antibacterial mechanisms, and do not easily result in the production of drug-resistant strains. Thus, the development of new antimicrobial peptides and their wide use instead of chemical antibiotics are of great significance to human health. In this review, we first summarized the relationship between the structures and functions of antimicrobial peptides. Then, we focused on examples, cathelicidins, a group of cationic antimicrobial peptides with multiple biological activities. Especially, cathelicidin BF30 or BF34, composed of 30 or 34 amino acids, were from the venom glands of the Bungarus fasciatus snake and were considered to be the most active antibacterial peptides among different cathelicidin members. Their solution structures determined by NMR are α-helixes, which are useful in designing new and stable peptides with similar framework, including stapple peptides by inducing chemical modifications in the sidechains of some residues, as well as cyclic peptides by inducing disulfide bond between cysteines in the sequences. |
| first_indexed | 2024-04-11T12:48:31Z |
| format | Article |
| id | doaj.art-5a71562edc484142819273b3cfa47064 |
| institution | Directory Open Access Journal |
| issn | 2772-5162 |
| language | English |
| last_indexed | 2024-04-11T12:48:31Z |
| publishDate | 2022-11-01 |
| publisher | KeAi Communications Co. Ltd. |
| record_format | Article |
| series | Magnetic Resonance Letters |
| spelling | doaj.art-5a71562edc484142819273b3cfa470642022-12-22T04:23:16ZengKeAi Communications Co. Ltd.Magnetic Resonance Letters2772-51622022-11-0124214223NMR assisted studies on the solution structures and functions of antimicrobial peptidesYaying Zhang0Chunyang Cao1College of Chemistry and Materials Science, Shanghai Normal University, 100 Guilin Road, Shanghai, 200234, China; State Key Laboratory of Bioorganic and Natural Product Chemistry, Center for Excellence in Molecular Synthesis, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 345 Lingling Road, Shanghai, 200032, ChinaCollege of Chemistry and Materials Science, Shanghai Normal University, 100 Guilin Road, Shanghai, 200234, China; State Key Laboratory of Bioorganic and Natural Product Chemistry, Center for Excellence in Molecular Synthesis, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 345 Lingling Road, Shanghai, 200032, China; Corresponding author. State Key Laboratory of Bioorganic and Natural Product Chemistry, Center for Excellence in Molecular Synthesis, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 345 Lingling Road, Shanghai, 200032, China.Microbial resistance has now become a global public health concern, and the spread of multidrug-resistant bacteria also threatens human health. Antimicrobial peptides (AMPs) are a class of small peptides with antibacterial, anti-inflammatory, anti-infective, anti-oxidation, anti-tumor, antiviral functions and immune regulation activities. Due to the small sizes, their structures are easily studied by nuclear magnetic resonance (NMR) techniques. Compared to traditional antibiotics, AMPs have specific antibacterial mechanisms, and do not easily result in the production of drug-resistant strains. Thus, the development of new antimicrobial peptides and their wide use instead of chemical antibiotics are of great significance to human health. In this review, we first summarized the relationship between the structures and functions of antimicrobial peptides. Then, we focused on examples, cathelicidins, a group of cationic antimicrobial peptides with multiple biological activities. Especially, cathelicidin BF30 or BF34, composed of 30 or 34 amino acids, were from the venom glands of the Bungarus fasciatus snake and were considered to be the most active antibacterial peptides among different cathelicidin members. Their solution structures determined by NMR are α-helixes, which are useful in designing new and stable peptides with similar framework, including stapple peptides by inducing chemical modifications in the sidechains of some residues, as well as cyclic peptides by inducing disulfide bond between cysteines in the sequences.http://www.sciencedirect.com/science/article/pii/S2772516222000390Nuclear magnetic resonanceAntimicrobial peptidesCathelicidinStructureFunction |
| spellingShingle | Yaying Zhang Chunyang Cao NMR assisted studies on the solution structures and functions of antimicrobial peptides Magnetic Resonance Letters Nuclear magnetic resonance Antimicrobial peptides Cathelicidin Structure Function |
| title | NMR assisted studies on the solution structures and functions of antimicrobial peptides |
| title_full | NMR assisted studies on the solution structures and functions of antimicrobial peptides |
| title_fullStr | NMR assisted studies on the solution structures and functions of antimicrobial peptides |
| title_full_unstemmed | NMR assisted studies on the solution structures and functions of antimicrobial peptides |
| title_short | NMR assisted studies on the solution structures and functions of antimicrobial peptides |
| title_sort | nmr assisted studies on the solution structures and functions of antimicrobial peptides |
| topic | Nuclear magnetic resonance Antimicrobial peptides Cathelicidin Structure Function |
| url | http://www.sciencedirect.com/science/article/pii/S2772516222000390 |
| work_keys_str_mv | AT yayingzhang nmrassistedstudiesonthesolutionstructuresandfunctionsofantimicrobialpeptides AT chunyangcao nmrassistedstudiesonthesolutionstructuresandfunctionsofantimicrobialpeptides |