Helical Antimicrobial Peptide Foldamers Containing Non-proteinogenic Amino Acids
- PMID: 33565721
- DOI: 10.1002/cmdc.202000940
Helical Antimicrobial Peptide Foldamers Containing Non-proteinogenic Amino Acids
Abstract
Antimicrobial peptides (AMPs) are potential novel therapeutic drugs against microbial infections. Most AMPs function by disrupting microbial membranes because of their amphipathic properties and ordered secondary structures. In this minireview, we describe recent efforts to develop helical AMP foldamers containing non-proteinogenic amino acids, such as α,α-disubstituted α-amino acids, β-amino acids, γ-amino acids, side-chain stapling and N-alkyl glycines.
Keywords: Gram-negative bacteria; Gram-positive bacteria; antimicrobial peptides; foldamers; helixes; non-proteinogenic amino acids.
© 2021 Wiley-VCH GmbH.
Similar articles
-
Rational Design of Helix-Stabilized Antimicrobial Peptide Foldamers Containing α,α-Disubstituted Amino Acids or Side-Chain Stapling.Chempluschem. 2020 Dec;85(12):2731-2736. doi: 10.1002/cplu.202000749. Chempluschem. 2020. PMID: 33369262
-
Structure-Activity Relationship Study of Helix-Stabilized Antimicrobial Peptides Containing Nonproteinogenic Amino Acids.ACS Biomater Sci Eng. 2023 Aug 14;9(8):4654-4661. doi: 10.1021/acsbiomaterials.3c00759. Epub 2023 Jul 24. ACS Biomater Sci Eng. 2023. PMID: 37486982
-
How Unnatural Amino Acids in Antimicrobial Peptides Change Interactions with Lipid Model Membranes.J Phys Chem B. 2024 Oct 10;128(40):9772-9784. doi: 10.1021/acs.jpcb.4c04152. Epub 2024 Sep 27. J Phys Chem B. 2024. PMID: 39328031 Free PMC article.
-
The world of beta- and gamma-peptides comprised of homologated proteinogenic amino acids and other components.Chem Biodivers. 2004 Aug;1(8):1111-239. doi: 10.1002/cbdv.200490087. Chem Biodivers. 2004. PMID: 17191902 Review.
-
Enhancing Antimicrobial Peptide Activity through Modifications of Charge, Hydrophobicity, and Structure.Int J Mol Sci. 2024 Oct 9;25(19):10821. doi: 10.3390/ijms251910821. Int J Mol Sci. 2024. PMID: 39409150 Free PMC article. Review.
Cited by
-
An intrinsically disordered antimicrobial peptide dendrimer from stereorandomized virtual screening.Cell Rep Phys Sci. 2022 Dec 21;3(12):101161. doi: 10.1016/j.xcrp.2022.101161. Cell Rep Phys Sci. 2022. PMID: 36632208 Free PMC article.
-
Foldamers controlled by functional triamino acids: structural investigation of α/γ-hybrid oligopeptides.Commun Chem. 2024 May 25;7(1):114. doi: 10.1038/s42004-024-01201-7. Commun Chem. 2024. PMID: 38796536 Free PMC article.
-
Structure-Activity Relationship Studies of Substitutions of Cationic Amino Acid Residues on Antimicrobial Peptides.Antibiotics (Basel). 2022 Dec 23;12(1):19. doi: 10.3390/antibiotics12010019. Antibiotics (Basel). 2022. PMID: 36671220 Free PMC article.
-
BSA Binding and Aggregate Formation of a Synthetic Amino Acid with Potential for Promoting Fibroblast Proliferation: An In Silico, CD Spectroscopic, DLS, and Cellular Study.Biomolecules. 2024 May 14;14(5):579. doi: 10.3390/biom14050579. Biomolecules. 2024. PMID: 38785986 Free PMC article.
-
To Fold or Not to Fold: Diastereomeric Optimization of an α-Helical Antimicrobial Peptide.J Med Chem. 2023 Jun 8;66(11):7570-7583. doi: 10.1021/acs.jmedchem.3c00460. Epub 2023 May 25. J Med Chem. 2023. PMID: 37227046 Free PMC article.
References
-
- N. Mookherjee, M. A. Anderson, H. P. Haagsman, D. J. Davidson, Nat. Rev. Drug Discovery 2020, 19, 311-332.
-
- C. D. Fjell, J. A. Hiss, R. E. Hancock, G. Schneider, Nat. Rev. Drug Discovery 2011, 11, 37-51.
-
- R. Spohn, L. Daruka, V. Lázár, A. Martins, F. Vidovics, G. Grézal, O. Méhi, B. Kintses, M. Számel, P. K. Jangir, B. Csörgő, Á. Györkei, Z. Bódi, A. Faragó, L. Bodai, I. Földesi, D. Kata, G. Maróti, B. Pap, R. Wirth, B. Papp, C. Pál, Nat. Commun. 2019, 10, 4538.
-
- J. Li, J. J. Koh, S. Liu, R. Lakshminarayanan, C. S. Verma, R. W. Beuerman, Front. Neurosci. 2017, 11, 73.
-
- M. Pushpanathan, P. Gunasekaran, J. Rajendhran, Int. J. Pept. Protein Res. 2013, 2013, 675391.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources
Medical