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Rational Design of Plant Hairpin-like Peptide EcAMP1: Structural–Functional Correlations to Reveal Antibacterial and Antifungal Activity
Plant antimicrobial peptides from the α-hairpinins family (hairpin-like peptides) are known to possess a wide range of biological activities. However, less is known about the structural determinants of their antimicrobial activity. Here, we suggest that spatial structure as well as surface charge an...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9182383/ https://www.ncbi.nlm.nih.gov/pubmed/35684491 http://dx.doi.org/10.3390/molecules27113554 |
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author | Barashkova, Anna S. Ryazantsev, Dmitry Y. Rogozhin, Eugene A. |
author_facet | Barashkova, Anna S. Ryazantsev, Dmitry Y. Rogozhin, Eugene A. |
author_sort | Barashkova, Anna S. |
collection | PubMed |
description | Plant antimicrobial peptides from the α-hairpinins family (hairpin-like peptides) are known to possess a wide range of biological activities. However, less is known about the structural determinants of their antimicrobial activity. Here, we suggest that spatial structure as well as surface charge and hydrophobicity level contribute to the antimicrobial properties of α-hairpinin EcAMP1 from barnyard grass (Echinochloa cruss-galli) seeds. To examine the role of the peptide spatial structure, two truncated forms of EcAMP1 restricted by inner and outer cysteine pairs were synthesized. It was shown that both truncated forms of EcAMP1 lost their antibacterial activity. In addition, their antifungal activity became weaker. To review the contribution of surface charge and hydrophobicity, another two peptides were designed. One of them carried single amino acid substitution from tryptophan to alanine residue at the 20th position. The second one represented a truncated form of the native EcAMP1 lacking six C-terminal residues. But the α-helix was kept intact. It was shown that the antifungal activity of both modified peptides weakened. Thereby we can conclude that the secondary structural integrity, hydrophobic properties, and surface charge all play roles in the antimicrobial properties of α-hairpinins. In addition, the antibacterial activity of cereal α-hairpinins against Gram-positive bacteria was described for the first time. This study expands on the knowledge of structure–function interactions in antimicrobial α-hairpinins. |
format | Online Article Text |
id | pubmed-9182383 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-91823832022-06-10 Rational Design of Plant Hairpin-like Peptide EcAMP1: Structural–Functional Correlations to Reveal Antibacterial and Antifungal Activity Barashkova, Anna S. Ryazantsev, Dmitry Y. Rogozhin, Eugene A. Molecules Article Plant antimicrobial peptides from the α-hairpinins family (hairpin-like peptides) are known to possess a wide range of biological activities. However, less is known about the structural determinants of their antimicrobial activity. Here, we suggest that spatial structure as well as surface charge and hydrophobicity level contribute to the antimicrobial properties of α-hairpinin EcAMP1 from barnyard grass (Echinochloa cruss-galli) seeds. To examine the role of the peptide spatial structure, two truncated forms of EcAMP1 restricted by inner and outer cysteine pairs were synthesized. It was shown that both truncated forms of EcAMP1 lost their antibacterial activity. In addition, their antifungal activity became weaker. To review the contribution of surface charge and hydrophobicity, another two peptides were designed. One of them carried single amino acid substitution from tryptophan to alanine residue at the 20th position. The second one represented a truncated form of the native EcAMP1 lacking six C-terminal residues. But the α-helix was kept intact. It was shown that the antifungal activity of both modified peptides weakened. Thereby we can conclude that the secondary structural integrity, hydrophobic properties, and surface charge all play roles in the antimicrobial properties of α-hairpinins. In addition, the antibacterial activity of cereal α-hairpinins against Gram-positive bacteria was described for the first time. This study expands on the knowledge of structure–function interactions in antimicrobial α-hairpinins. MDPI 2022-05-31 /pmc/articles/PMC9182383/ /pubmed/35684491 http://dx.doi.org/10.3390/molecules27113554 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/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/). |
spellingShingle | Article Barashkova, Anna S. Ryazantsev, Dmitry Y. Rogozhin, Eugene A. Rational Design of Plant Hairpin-like Peptide EcAMP1: Structural–Functional Correlations to Reveal Antibacterial and Antifungal Activity |
title | Rational Design of Plant Hairpin-like Peptide EcAMP1: Structural–Functional Correlations to Reveal Antibacterial and Antifungal Activity |
title_full | Rational Design of Plant Hairpin-like Peptide EcAMP1: Structural–Functional Correlations to Reveal Antibacterial and Antifungal Activity |
title_fullStr | Rational Design of Plant Hairpin-like Peptide EcAMP1: Structural–Functional Correlations to Reveal Antibacterial and Antifungal Activity |
title_full_unstemmed | Rational Design of Plant Hairpin-like Peptide EcAMP1: Structural–Functional Correlations to Reveal Antibacterial and Antifungal Activity |
title_short | Rational Design of Plant Hairpin-like Peptide EcAMP1: Structural–Functional Correlations to Reveal Antibacterial and Antifungal Activity |
title_sort | rational design of plant hairpin-like peptide ecamp1: structural–functional correlations to reveal antibacterial and antifungal activity |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9182383/ https://www.ncbi.nlm.nih.gov/pubmed/35684491 http://dx.doi.org/10.3390/molecules27113554 |
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