Identification of a novel storage glycine-rich peptide from guava (Psidium guajava) seeds with activity against Gram-negative bacteria
Open accessAbstract
Bacterial pathogens cause an expressive negative impact worldwide on human health, with ever increasing treatment costs. A significant rise in resistance to commercial antibiotics has been observed in pathogenic bacteria responsible for urinary and gastro-intestinal infections. Towards the development of novel approaches to control such common infections, a number of defense peptides with antibacterial activities have been characterized. In this report, the peptide Pg-AMP1 was isolated from guava seeds (Psidium guajava) and purified using a Red-Sepharose Cl-6B affinity column followed by a reversed-phase HPLC (Vydac C18-TP). Pg-AMP1 showed no inhibitory activity against fungi, but resulted in a clear growth reduction in Klebsiella sp. and Proteus sp., which are the principal pathogens involved in urinary and gastro-intestinal hospital infections. SDS-PAGE and mass spectrometry (MALDI-ToF) characterized Pg-AMP1 a monomer with a molecular mass of 6029.34Da and small quantities of a homodimer. Amino acid sequencing revealed clear identity to the plant glycine-rich protein family, with Pg-AMP1 the first such protein with activity towards Gram-negative bacteria. Furthermore, Pg-AMP1 showed a 3D structural homology to an enterotoxin from Escherichia coli, and other antibacterial proteins, revealing that it might act by formation of a dimer. Pg-AMP1 shows potential, in a near future, to contribute to development of novel antibiotics from natural sources.
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Cn-AMP1 has a possible region that could interact with negative surfaces, including bacterial membranes or nucleic acids.
“Fig. 4D shows a possible Cn-AMP1 region that could show clear interactivity with negative surfaces, including bacterial membranes or nucleic acids, which are common targets for antimicrobial peptides [28].”
From Structural insights into <i>Cn</i>‐AMP1, a short disulfide‐free multifunctional peptide from green coconut water (2015) · cites this paper as [28]
Glycines in Cn-AMP1 could be important to antimicrobial function because they improve peptide flexibility.
“suggesting that glycines from Cn-AMP1 could be important to antimicrobial function since they improve peptide flexibility.”
From Structural insights into <i>Cn</i>‐AMP1, a short disulfide‐free multifunctional peptide from green coconut water (2015) · cites this paper as [28]
The role of glycines in peptide flexibility was previously observed for other linear peptides.
“The role of glycines in peptide flexibility was previously observed for other linear peptides.”
From Structural insights into <i>Cn</i>‐AMP1, a short disulfide‐free multifunctional peptide from green coconut water (2015) · cites this paper as [28]
A glycine-rich antimicrobial peptide from guava seeds has numerous glycines that improve flexibility and seem involved in bactericidal activity.
“Moreover, a glycine-rich antimicrobial peptide isolated from guava seeds also showed numerous glycines that improve flexibility and seem to be closely involved in bactericidal activity [28]”
From Structural insights into <i>Cn</i>‐AMP1, a short disulfide‐free multifunctional peptide from green coconut water (2015) · cites this paper as [28]
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Mandal, S. M., Dey, S., Mandal, M., Sarkar, S., Maria-Neto, S., & Franco, O. L. (2009) · Peptides · doi:10.1016/j.peptides.2008.12.001 · Cited by 136 · see citing works
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<i>Cn</i>‐AMP1: A new promiscuous peptide with potential for microbial infections treatment
Silva, O. N., Porto, W. F., Migliolo, L., Mandal, S. M., Gomes, D. G., Holanda, H. H. S., Silva, R. S. P., Dias, S. C., Costa, M. P., Costa, C. R., et al. (2012) · Peptide Science · doi:10.1002/bip.22071 · Cited by 51 · see citing works
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- Authors
- Pelegrini, P. B., Murad, A. M., Silva, L. P., dos Santos, R. C. P., Costa, F. T., Tagliari, P. D., Bloch Jr, C., Noronha, E. F., Miller, R. N. G., & Franco, O. L.
- Affiliations
- Universidade Católica de Brasília (BR)
- Embrapa (BR)
- Venue
- Peptides
- Publisher
- Elsevier BV
- Published
- 2008-08
- Volume
- 29
- Issue
- 8
- Pages
- 1271-1279
- ISSN
- 0196-9781 (ISSN-L)
- OpenAlex
- W1971932800
- Cited by
- 136
- References
- 1
- Citations by year
- 2026: 5 · 2025: 6 · 2024: 14 · 2023: 8 · 2022: 14 · 2021: 6 · 2020: 3 · 2019: 12 · 2018: 11 · 2017: 7 · 2016: 3 · 2015: 5 · 2014: 9 · 2013: 6 · 2012: 5
- FWCI
- 6.61
- Type
- journal article
- Language
- en
- Open access
- Licence
- Locations
- Peptides (publishedVersion)
- PubMed (publishedVersion)
- LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas) (publishedVersion, other-oa)
- Topics
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Physical Sciences › Chemistry › Organic Chemistry › Antimicrobial agents and applications
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Psidium guajava Extracts and Applications
- Keywords
- guava seeds, guava, antibacterial peptides, Gram-negative bacteria, Klebsiella, Proteus, urinary tract infection, gastrointestinal infections, antibiotic resistance, plant defense peptides, peptide dimerization, natural antibiotics
- MeSH terms
- Amino Acid Sequence, Anti-Infective Agents, Electrophoresis, Polyacrylamide Gel, Glycine, Gram-Negative Bacteria, Microbial Sensitivity Tests, Models, Molecular, Molecular Sequence Data, Plant Proteins, Protein Conformation, Seeds, Sequence Alignment, Psidium
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