Natural and Synthetic Halogenated Amino Acids-Structural and Bioactive Features in Antimicrobial Peptides and Peptidomimetics
The 3D structure and surface characteristics of proteins and peptides are crucial for interactions with receptors or ligands and can be modified to some extent to modulate their biological roles and pharmacological activities. The introduction of halogen atoms on the side-chains of amino acids is a...
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| Veröffentlicht in: | Molecules (Basel, Switzerland) Switzerland), 2021-12, Vol.26 (23), p.7401 |
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| creator | Mardirossian, Mario Rubini, Marina Adamo, Mauro F A Scocchi, Marco Saviano, Michele Tossi, Alessandro Gennaro, Renato Caporale, Andrea |
| description | The 3D structure and surface characteristics of proteins and peptides are crucial for interactions with receptors or ligands and can be modified to some extent to modulate their biological roles and pharmacological activities. The introduction of halogen atoms on the side-chains of amino acids is a powerful tool for effecting this type of tuning, influencing both the physico-chemical and structural properties of the modified polypeptides, helping to first dissect and then rationally modify features that affect their mode of action. This review provides examples of the influence of different types of halogenation in amino acids that replace native residues in proteins and peptides. Examples of synthetic strategies for obtaining halogenated amino acids are also provided, focusing on some representative compounds and their biological effects. The role of halogenation in native and designed antimicrobial peptides (AMPs) and their mimetics is then discussed. These are in the spotlight for the development of new antimicrobial drugs to counter the rise of antibiotic-resistant pathogens. AMPs represent an interesting model to study the role that natural halogenation has on their mode of action and also to understand how artificially halogenated residues can be used to rationally modify and optimize AMPs for pharmaceutical purposes. |
| doi_str_mv | 10.3390/molecules26237401 |
| format | Article |
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The introduction of halogen atoms on the side-chains of amino acids is a powerful tool for effecting this type of tuning, influencing both the physico-chemical and structural properties of the modified polypeptides, helping to first dissect and then rationally modify features that affect their mode of action. This review provides examples of the influence of different types of halogenation in amino acids that replace native residues in proteins and peptides. Examples of synthetic strategies for obtaining halogenated amino acids are also provided, focusing on some representative compounds and their biological effects. The role of halogenation in native and designed antimicrobial peptides (AMPs) and their mimetics is then discussed. These are in the spotlight for the development of new antimicrobial drugs to counter the rise of antibiotic-resistant pathogens. AMPs represent an interesting model to study the role that natural halogenation has on their mode of action and also to understand how artificially halogenated residues can be used to rationally modify and optimize AMPs for pharmaceutical purposes.</description><identifier>ISSN: 1420-3049</identifier><identifier>EISSN: 1420-3049</identifier><identifier>DOI: 10.3390/molecules26237401</identifier><identifier>PMID: 34885985</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Amino acids ; Anti-Bacterial Agents - chemistry ; Anti-Bacterial Agents - pharmacology ; Antibiotic resistance ; Antibiotics ; Antiinfectives and antibacterials ; Antimicrobial agents ; Antimicrobial peptides ; antimicrobial peptides (AMPs) ; Antimicrobial Peptides - chemistry ; Biological effects ; bromo-tryptophan ; Carbon ; Drug development ; Enzymes ; Fluorine ; fluoro amino acids ; fluoro-proline ; Gram-Negative Bacteria - drug effects ; Gram-Positive Bacteria - drug effects ; Halogenation ; Halogens - chemistry ; Humans ; Microbial Sensitivity Tests ; Mode of action ; Peptides ; Peptidomimetics ; Peptidomimetics - chemistry ; Peptidomimetics - metabolism ; Peptoids - chemistry ; Polypeptides ; Proline - analogs & derivatives ; Proline - chemistry ; Protein folding ; Proteins ; Residues ; Review ; Signal transduction ; Structure-Activity Relationship ; Surface properties</subject><ispartof>Molecules (Basel, Switzerland), 2021-12, Vol.26 (23), p.7401</ispartof><rights>2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). 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The introduction of halogen atoms on the side-chains of amino acids is a powerful tool for effecting this type of tuning, influencing both the physico-chemical and structural properties of the modified polypeptides, helping to first dissect and then rationally modify features that affect their mode of action. This review provides examples of the influence of different types of halogenation in amino acids that replace native residues in proteins and peptides. Examples of synthetic strategies for obtaining halogenated amino acids are also provided, focusing on some representative compounds and their biological effects. The role of halogenation in native and designed antimicrobial peptides (AMPs) and their mimetics is then discussed. These are in the spotlight for the development of new antimicrobial drugs to counter the rise of antibiotic-resistant pathogens. AMPs represent an interesting model to study the role that natural halogenation has on their mode of action and also to understand how artificially halogenated residues can be used to rationally modify and optimize AMPs for pharmaceutical purposes.</description><subject>Amino acids</subject><subject>Anti-Bacterial Agents - chemistry</subject><subject>Anti-Bacterial Agents - pharmacology</subject><subject>Antibiotic resistance</subject><subject>Antibiotics</subject><subject>Antiinfectives and antibacterials</subject><subject>Antimicrobial agents</subject><subject>Antimicrobial peptides</subject><subject>antimicrobial peptides (AMPs)</subject><subject>Antimicrobial Peptides - chemistry</subject><subject>Biological effects</subject><subject>bromo-tryptophan</subject><subject>Carbon</subject><subject>Drug development</subject><subject>Enzymes</subject><subject>Fluorine</subject><subject>fluoro amino acids</subject><subject>fluoro-proline</subject><subject>Gram-Negative Bacteria - drug effects</subject><subject>Gram-Positive Bacteria - 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chemistry</topic><topic>Anti-Bacterial Agents - pharmacology</topic><topic>Antibiotic resistance</topic><topic>Antibiotics</topic><topic>Antiinfectives and antibacterials</topic><topic>Antimicrobial agents</topic><topic>Antimicrobial peptides</topic><topic>antimicrobial peptides (AMPs)</topic><topic>Antimicrobial Peptides - chemistry</topic><topic>Biological effects</topic><topic>bromo-tryptophan</topic><topic>Carbon</topic><topic>Drug development</topic><topic>Enzymes</topic><topic>Fluorine</topic><topic>fluoro amino acids</topic><topic>fluoro-proline</topic><topic>Gram-Negative Bacteria - drug effects</topic><topic>Gram-Positive Bacteria - drug effects</topic><topic>Halogenation</topic><topic>Halogens - chemistry</topic><topic>Humans</topic><topic>Microbial Sensitivity Tests</topic><topic>Mode of action</topic><topic>Peptides</topic><topic>Peptidomimetics</topic><topic>Peptidomimetics - chemistry</topic><topic>Peptidomimetics - metabolism</topic><topic>Peptoids - chemistry</topic><topic>Polypeptides</topic><topic>Proline - 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The introduction of halogen atoms on the side-chains of amino acids is a powerful tool for effecting this type of tuning, influencing both the physico-chemical and structural properties of the modified polypeptides, helping to first dissect and then rationally modify features that affect their mode of action. This review provides examples of the influence of different types of halogenation in amino acids that replace native residues in proteins and peptides. Examples of synthetic strategies for obtaining halogenated amino acids are also provided, focusing on some representative compounds and their biological effects. The role of halogenation in native and designed antimicrobial peptides (AMPs) and their mimetics is then discussed. These are in the spotlight for the development of new antimicrobial drugs to counter the rise of antibiotic-resistant pathogens. 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| subjects | Amino acids Anti-Bacterial Agents - chemistry Anti-Bacterial Agents - pharmacology Antibiotic resistance Antibiotics Antiinfectives and antibacterials Antimicrobial agents Antimicrobial peptides antimicrobial peptides (AMPs) Antimicrobial Peptides - chemistry Biological effects bromo-tryptophan Carbon Drug development Enzymes Fluorine fluoro amino acids fluoro-proline Gram-Negative Bacteria - drug effects Gram-Positive Bacteria - drug effects Halogenation Halogens - chemistry Humans Microbial Sensitivity Tests Mode of action Peptides Peptidomimetics Peptidomimetics - chemistry Peptidomimetics - metabolism Peptoids - chemistry Polypeptides Proline - analogs & derivatives Proline - chemistry Protein folding Proteins Residues Review Signal transduction Structure-Activity Relationship Surface properties |
| title | Natural and Synthetic Halogenated Amino Acids-Structural and Bioactive Features in Antimicrobial Peptides and Peptidomimetics |
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