Biologically active and antimicrobial peptides from plants

doi:10.1155/2015/102129

Review

. 2015:2015:102129.

doi: 10.1155/2015/102129. Epub 2015 Mar 1.

Biologically active and antimicrobial peptides from plants

Carlos E Salas¹, Jesus A Badillo-Corona², Guadalupe Ramírez-Sotelo², Carmen Oliver-Salvador²

Affiliations

¹ Departamento de Bioquímica, Universidade Federal de Minas Gerais, 31270-901 Belo Horizonte, Brazil.
² Unidad Profesional Interdisciplinaria de Biotecnología, Instituto Politécnico Nacional, Avenida Acueducto S/N, Colonia Barrio La Laguna Ticomán, 07320 Mexico City, Mexico.

PMID: 25815307
PMCID: PMC4359881
DOI: 10.1155/2015/102129

Review

Biologically active and antimicrobial peptides from plants

Carlos E Salas et al. Biomed Res Int. 2015.

. 2015:2015:102129.

doi: 10.1155/2015/102129. Epub 2015 Mar 1.

Authors

Carlos E Salas¹, Jesus A Badillo-Corona², Guadalupe Ramírez-Sotelo², Carmen Oliver-Salvador²

Affiliations

¹ Departamento de Bioquímica, Universidade Federal de Minas Gerais, 31270-901 Belo Horizonte, Brazil.
² Unidad Profesional Interdisciplinaria de Biotecnología, Instituto Politécnico Nacional, Avenida Acueducto S/N, Colonia Barrio La Laguna Ticomán, 07320 Mexico City, Mexico.

PMID: 25815307
PMCID: PMC4359881
DOI: 10.1155/2015/102129

Abstract

Bioactive peptides are part of an innate response elicited by most living forms. In plants, they are produced ubiquitously in roots, seeds, flowers, stems, and leaves, highlighting their physiological importance. While most of the bioactive peptides produced in plants possess microbicide properties, there is evidence that they are also involved in cellular signaling. Structurally, there is an overall similarity when comparing them with those derived from animal or insect sources. The biological action of bioactive peptides initiates with the binding to the target membrane followed in most cases by membrane permeabilization and rupture. Here we present an overview of what is currently known about bioactive peptides from plants, focusing on their antimicrobial activity and their role in the plant signaling network and offering perspectives on their potential application.

PubMed Disclaimer

Cited by

Toxic proteins in plants.
Dang L, Van Damme EJM. Dang L, et al. Phytochemistry. 2015 Sep;117:51-64. doi: 10.1016/j.phytochem.2015.05.020. Epub 2015 Jun 7. Phytochemistry. 2015. PMID: 26057229 Free PMC article. Review.
Biologia futura: medicinal plants-derived bioactive peptides in functional perspective-a review.
Meena S, Kanthaliya B, Joshi A, Khan F, Arora J. Meena S, et al. Biol Futur. 2020 Sep;71(3):195-208. doi: 10.1007/s42977-020-00042-4. Epub 2020 Sep 5. Biol Futur. 2020. PMID: 34554518 Review.
Characterisation of Biologically Active Hydrolysates and Peptide Fractions of Vacuum Packaging String Bean (Phaseolus vulgaris L.).
Jakubczyk A, Karaś M, Stanikowski P, Rutkowska B, Dziedzic M, Zielińska E, Szychowski KA, Binduga UE, Rybczyńska-Tkaczyk K, Baraniak B. Jakubczyk A, et al. Foods. 2020 Jun 28;9(7):842. doi: 10.3390/foods9070842. Foods. 2020. PMID: 32605271 Free PMC article.
A novel recombinant javanicin with dual antifungal and anti-proliferative activities.
Orrapin S, Intorasoot A, Roytrakul S, Dechsupa N, Kantapan J, Onphat Y, Srimek C, Sitthidet Tharinjaroen C, Anukool U, Butr-Indr B, Phunpae P, Intorasoot S. Orrapin S, et al. Sci Rep. 2019 Dec 5;9(1):18417. doi: 10.1038/s41598-019-55044-7. Sci Rep. 2019. PMID: 31804594 Free PMC article.
Plant-Derived Antimicrobial Peptides as Potential Antiviral Agents in Systemic Viral Infections.
Mammari N, Krier Y, Albert Q, Devocelle M, Varbanov M, On Behalf Of The Oemonom. Mammari N, et al. Pharmaceuticals (Basel). 2021 Aug 6;14(8):774. doi: 10.3390/ph14080774. Pharmaceuticals (Basel). 2021. PMID: 34451871 Free PMC article. Review.

See all "Cited by" articles

References

1. Park I. Y., Cho J. H., Kim K. S., Kim Y.-B., Kim M. S., Kim S. C. Helix stability confers salt resistance upon helical antimicrobial peptides. The Journal of Biological Chemistry. 2004;279(14):13896–13901. doi: 10.1074/jbc.M311418200. - DOI - PubMed
1. Wang Z., Wang G. APD: the antimicrobial peptide database. Nucleic Acids Research. 2004;32:D590–D592. doi: 10.1093/nar/gkh025. - DOI - PMC - PubMed
1. Zeya H. I., Spitznagel J. K. Antibacterial and enzymic basic proteins from leukocyte lysosomes: separation and identification. Science. 1963;142(3595):1085–1087. doi: 10.1126/science.142.3595.1085. - DOI - PubMed
1. Hultmark D., Steiner H., Rasmuson T., Boman H. G. Insect immunity. Purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of Hyalophora cecropia . European Journal of Biochemistry. 1980;106(1):7–16. - PubMed
1. Yamaguchi Y., Huffaker A. Endogenous peptide elicitors in higher plants. Current Opinion in Plant Biology. 2011;14(4):351–357. doi: 10.1016/j.pbi.2011.05.001. - DOI - PubMed

Publication types

Actions
Actions

MeSH terms

Actions
Actions
Actions
Actions
Actions
Actions
Actions

Substances

Actions
Actions

LinkOut - more resources

Full Text Sources
Other Literature Sources
- scite Smart Citations

[1] Park I. Y., Cho J. H., Kim K. S., Kim Y.-B., Kim M. S., Kim S. C. Helix stability confers salt resistance upon helical antimicrobial peptides. The Journal of Biological Chemistry. 2004;279(14):13896–13901. doi: 10.1074/jbc.M311418200. - DOI - PubMed

[2] Park I. Y., Cho J. H., Kim K. S., Kim Y.-B., Kim M. S., Kim S. C. Helix stability confers salt resistance upon helical antimicrobial peptides. The Journal of Biological Chemistry. 2004;279(14):13896–13901. doi: 10.1074/jbc.M311418200. - DOI - PubMed

[3] Wang Z., Wang G. APD: the antimicrobial peptide database. Nucleic Acids Research. 2004;32:D590–D592. doi: 10.1093/nar/gkh025. - DOI - PMC - PubMed

[4] Wang Z., Wang G. APD: the antimicrobial peptide database. Nucleic Acids Research. 2004;32:D590–D592. doi: 10.1093/nar/gkh025. - DOI - PMC - PubMed

[5] Zeya H. I., Spitznagel J. K. Antibacterial and enzymic basic proteins from leukocyte lysosomes: separation and identification. Science. 1963;142(3595):1085–1087. doi: 10.1126/science.142.3595.1085. - DOI - PubMed

[6] Zeya H. I., Spitznagel J. K. Antibacterial and enzymic basic proteins from leukocyte lysosomes: separation and identification. Science. 1963;142(3595):1085–1087. doi: 10.1126/science.142.3595.1085. - DOI - PubMed

[7] Hultmark D., Steiner H., Rasmuson T., Boman H. G. Insect immunity. Purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of Hyalophora cecropia . European Journal of Biochemistry. 1980;106(1):7–16. - PubMed

[8] Hultmark D., Steiner H., Rasmuson T., Boman H. G. Insect immunity. Purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of Hyalophora cecropia . European Journal of Biochemistry. 1980;106(1):7–16. - PubMed

[9] Yamaguchi Y., Huffaker A. Endogenous peptide elicitors in higher plants. Current Opinion in Plant Biology. 2011;14(4):351–357. doi: 10.1016/j.pbi.2011.05.001. - DOI - PubMed

[10] Yamaguchi Y., Huffaker A. Endogenous peptide elicitors in higher plants. Current Opinion in Plant Biology. 2011;14(4):351–357. doi: 10.1016/j.pbi.2011.05.001. - DOI - PubMed

Save citation to file

Email citation

Add to Collections

Add to My Bibliography

Your saved search

Create a file for external citation management software

Your RSS Feed

Biologically active and antimicrobial peptides from plants

Affiliations

Biologically active and antimicrobial peptides from plants

Authors

Affiliations

Abstract

Similar articles

Cited by

References

Publication types

MeSH terms

Substances

LinkOut - more resources

Full Text Sources

Other Literature Sources