Natural and Synthetic Halogenated Amino Acids-Structural and Bioactive Features in Antimicrobial Peptides and Peptidomimetics.

Tytuł:: Natural and Synthetic Halogenated Amino Acids-Structural and Bioactive Features in Antimicrobial Peptides and Peptidomimetics.
Autorzy:: Mardirossian M; Department of Medicine, Surgery and Health Sciences, University of Trieste, Piazza dell'Ospitale, 1, 34125 Trieste, Italy.
Rubini M; School of Chemistry, University College Dublin, Belfield, Dublin 4, Ireland.
Adamo MFA; Department of Chemistry, Centre for Synthesis and Chemical Biology (CSCB), RCSI, 123 St. Stephens Green, Dublin 2, Ireland.
Scocchi M; Department of Life Sciences, University of Trieste, Via L. Giorgieri, 5, Q Building, 34127 Trieste, Italy.
Saviano M; Institute of Crystallography (IC), National Research Council (CNR), Via Amendola, 122, 70126 Bari, Italy.
Tossi A; Department of Life Sciences, University of Trieste, Via L. Giorgieri, 5, Q Building, 34127 Trieste, Italy.
Gennaro R; Department of Life Sciences, University of Trieste, Via L. Giorgieri, 5, Q Building, 34127 Trieste, Italy.
Caporale A; Institute of Crystallography (IC), National Research Council (CNR), c/o Area Science Park, S.S. 14 Km 163.5, Basovizza, 34149 Trieste, Italy.
Źródło:: Molecules (Basel, Switzerland) [Molecules] 2021 Dec 06; Vol. 26 (23). Date of Electronic Publication: 2021 Dec 06.
Typ publikacji:: Journal Article; Review
Język:: English
Imprint Name(s):: Original Publication: Basel, Switzerland : MDPI, c1995-
MeSH Terms:: Halogenation*
Anti-Bacterial Agents/*chemistry
Antimicrobial Peptides/*chemistry
Halogens/*chemistry
Peptidomimetics/*metabolism
Proline/*analogs & derivatives
Anti-Bacterial Agents/pharmacology ; Gram-Negative Bacteria/drug effects ; Gram-Positive Bacteria/drug effects ; Humans ; Microbial Sensitivity Tests ; Peptidomimetics/chemistry ; Peptoids/chemistry ; Proline/chemistry ; Structure-Activity Relationship
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Contributed Indexing:: Keywords: antimicrobial peptides (AMPs); bromo-tryptophan; fluoro amino acids; fluoro-proline; halogenation; peptides; structure-activity relationship; α- and β-peptoids
Substance Nomenclature:: 0 (Anti-Bacterial Agents)
0 (Antimicrobial Peptides)
0 (Halogens)
0 (Peptidomimetics)
0 (Peptoids)
0 (fluoro-proline)
9DLQ4CIU6V (Proline)
Entry Date(s):: Date Created: 20211210 Date Completed: 20220214 Latest Revision: 20220214
Update Code:: 20240105
PubMed Central ID:: PMC8659048
DOI:: 10.3390/molecules26237401
PMID:: 34885985
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Pełny tekst

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.

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