A C-terminal cationic fragment derived from an arginine-rich peptide exhibits in vitro antibacterial and anti-plasmodial activities governed by its secondary structure properties

Lesmes, Liliana Patricia; Bohorquez, Magda Yenith; Carreño, Luisa Fernanda; Patarroyo, Manuel E.; Lozano, José Manuel

doi:10.1016/j.peptides.2009.08.011

Cited by 10 publications

(8 citation statements)

References 36 publications

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“…It consists of four arginine clusters. Radial diffusion assay has shown that a single arginine-rich domain (RRRR) is sufficient for antimicrobial activity, especially against Gram-negative bacteria [16]. Unlike protamine, the arginine-rich domain of HBc147-183, such as ARD I–II and ARD III–IV, were not sufficient for the antimicrobial activity.…”

Section: Discussionmentioning

confidence: 99%

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Identification of a Novel Antimicrobial Peptide from Human Hepatitis B Virus Core Protein Arginine-Rich Domain (ARD)

Chen

Chang

et al. 2013

PLoS Pathog

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The rise of multidrug-resistant (MDR) pathogens causes an increasing challenge to public health. Antimicrobial peptides are considered a possible solution to this problem. HBV core protein (HBc) contains an arginine-rich domain (ARD) at its C-terminus, which consists of 16 arginine residues separated into four clusters (ARD I to IV). In this study, we demonstrated that the peptide containing the full-length ARD I–IV (HBc147-183) has a broad-spectrum antimicrobial activity at micro-molar concentrations, including some MDR and colistin (polymyxin E)-resistant Acinetobacter baumannii. Furthermore, confocal fluorescence microscopy and SYTOX Green uptake assay indicated that this peptide killed Gram-negative and Gram-positive bacteria by membrane permeabilization or DNA binding. In addition, peptide ARD II–IV (HBc153-176) and ARD I–III (HBc147-167) were found to be necessary and sufficient for the activity against P. aeruginosa and K. peumoniae. The antimicrobial activity of HBc ARD peptides can be attenuated by the addition of LPS. HBc ARD peptide was shown to be capable of direct binding to the Lipid A of lipopolysaccharide (LPS) in several in vitro binding assays. Peptide ARD I–IV (HBc147-183) had no detectable cytotoxicity in various tissue culture systems and a mouse animal model. In the mouse model by intraperitoneal (i.p.) inoculation with Staphylococcus aureus, timely treatment by i.p. injection with ARD peptide resulted in 100-fold reduction of bacteria load in blood, liver and spleen, as well as 100% protection of inoculated animals from death. If peptide was injected when bacterial load in the blood reached its peak, the protection rate dropped to 40%. Similar results were observed in K. peumoniae using an IVIS imaging system. The finding of anti-microbial HBc ARD is discussed in the context of commensal gut microbiota, development of intrahepatic anti-viral immunity and establishment of chronic infection with HBV. Our current results suggested that HBc ARD could be a new promising antimicrobial peptide.

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Section: Discussionmentioning

confidence: 99%

“…To date, more than one thousand AMPs have been identified in various species including plants, insects, fish, frogs, and mammals [8], [9], [10], [11], [12], [13]. Although their sequences vary greatly, certain amino acids such as cysteine, lysine, proline or arginine are key compositions of AMPs [12], [14], [15], [16], [17].…”

Section: Introductionmentioning

confidence: 99%

Identification of a Novel Antimicrobial Peptide from Human Hepatitis B Virus Core Protein Arginine-Rich Domain (ARD)

Chen

Chang

et al. 2013

PLoS Pathog

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“…Protamine is a natural cationic antimicrobial peptide (CAP) composed mainly of strongly basic arginine residues. Protamine has broad-spectrum antimicrobial activities against a wide range of gram-positive and gram-negative bacteria [ 11 , 12 , 13 , 14 ]. The antimicrobial mechanism of action for protamine is believed to be the electrostatic attraction between the cationic peptide and the negatively-charged cell envelope, which kills susceptible bacteria due to cell envelope lysis and leakage of K + , adenosine triphosphate (ATP), and intracellular enzymes [ 15 , 16 ].…”

Section: Introductionmentioning

confidence: 99%

Antibacterial Effects of Chitosan/Cationic Peptide Nanoparticles

Tamara

Lin

et al. 2018

Nanomaterials

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This study attempted to develop chitosan-based nanoparticles with increased stability and antibacterial activity. The chitosan/protamine hybrid nanoparticles were formed based on an ionic gelation method by mixing chitosan with protamine and subsequently cross-linking the mixtures with sodium tripolyphosphate (TPP). The effects of protamine on the chemical structures, physical properties, and antibacterial activities of the hybrid nanoparticles were investigated. The antibacterial experiments demonstrated that the addition of protamine (125 µg/mL) in the hybrid nanoparticles (500 µg/mL chitosan and 166.67 µg/mL TPP) improved the antimicrobial specificity with the minimum inhibitory concentration (MIC) value of 31.25 µg/mL towards Escherichia coli (E. coli), while the MIC value was higher than 250 µg/mL towards Bacillus cereus. The chitosan/protamine hybrid nanoparticles induced the formation of biofilm-like structure in B. cereus and non-motile-like structure in E. coli. The detection of bacterial cell ruptures showed that the inclusion of protamine in the hybrid nanoparticles caused different membrane permeability compared to chitosan nanoparticles and chitosan alone. The chitosan/protamine nanoparticles also exhibited lower binding affinity towards B. cereus than E. coli. The results suggested that the hybridization of chitosan with protamine improved the antibacterial activity of chitosan nanoparticles towards pathogenic E. coli, but the inhibitory effect against probiotic B. cereus was significantly reduced.

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“…As all antimicrobial peptides had been tested for their in vitro activity against two representative Leishmania species and their individual conformational profiles had been previously obtained by circular dichroism (CD) experiments [17], it was decided to analyse the most active ones by in silico molecular modelling. Coordinates and data for each peptide were thus downloaded from the Protein Data Bank (PDB) (http://www.rcsb.org/pdb/home/home.do) regarding bombinin (PBD code 2AP8), dermaseptin-S1 (PBD code 2DD6), mastoparan (PDB 1D7N) and tachyplesin (PDB 1WO0) 3D structure determined by NMR or X-ray crystallography and molecularly modelled.…”

Section: (V) Panamensis and L (L) Majormentioning

confidence: 99%

“…The secondary structure profile of every synthesised peptide was then identified by circular dichroism (CD) experiments [17].…”

Section: Introductionmentioning

confidence: 99%

Cationic Peptides Harboring Antibiotic Capacity is Selective for Leishmania Panamensis and Leishmania Major

Lozano¹

2014

J Microb Biochem Technol

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The fairly recent appearance of Leishmania resistance to currently-used therapy has led to the search for new therapeutic strategies. This work was thus aimed at evaluating the in vitro effect of 18 cationic synthetic antimicrobial peptides for antileishmanial and cytotoxic and haemolytic activity. The viability of murine (J774) and human (U937), peripheral blood monocytes, HeLa and HepG2 cells and L. (V) panamensis and L. (L) major promastigotes was then ascertained using the aforementioned peptides. All antimicrobial peptides were synthesised and each cell and parasite line was treated with different peptide concentrations. Melittin, bombinin, mastoparan 8 (MP-8), MP-X and dermaseptin-S1 reduced human and murine host cells' viability at greater concentrations than pentamidine isethionate, human peripheral blood and U937 monocytes being the most sensitive to peptide action. Melittin had a toxic effect on all the cells evaluated in this study and L. (L) major was more sensitive than L. (V) panamensis to peptide effect. As MP-8, bombinin, dermaseptin-S1 and tracheal antimicrobial peptide (TAP) were active against both parasite species, and tachyplesin 1 and polystes MA selectively so for L. (L) major, they were selected as being promising as they had a >1 selectivity index (SI) and greater than 50 µg/mL haemolytic concentration (HC50), suggesting that they should continue to be studied in in vitro and in vivo infection assays as there have been no previous reports of MP-8, bombinin, TAP and Polystes MA activity regarding L. (V) panamensis and L. (L) major.

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A C-terminal cationic fragment derived from an arginine-rich peptide exhibits in vitro antibacterial and anti-plasmodial activities governed by its secondary structure properties

Cited by 10 publications

References 36 publications

Identification of a Novel Antimicrobial Peptide from Human Hepatitis B Virus Core Protein Arginine-Rich Domain (ARD)

Identification of a Novel Antimicrobial Peptide from Human Hepatitis B Virus Core Protein Arginine-Rich Domain (ARD)

Antibacterial Effects of Chitosan/Cationic Peptide Nanoparticles

Cationic Peptides Harboring Antibiotic Capacity is Selective for Leishmania Panamensis and Leishmania Major

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