scholarly journals COMBINED ANTIBACTERIAL ACTION OF SALIVARY CATIONIC PROLINE-RICH PEPTIDES AND ANTIMICROBIAL PEPTIDES

2019 ◽  
Vol 19 (1S) ◽  
pp. 180-181
Author(s):  
M S Sukhareva ◽  
P M Kopeykin ◽  
M S Zharkova ◽  
O V Shamova
Keyword(s):  
Oral Cavity ◽  
Antimicrobial Peptides ◽  
Solid Phase ◽  
Biological Fluid ◽  
Antibacterial Action ◽  
Main Function ◽  
Histatin 5 ◽  
Minimal Inhibitory Concentrations ◽  
Antimicrobial Protection ◽  
Combined Action

Saliva is an important biological fluid that reflects human’s health. Its main function is protection of the oral cavity from pathogens. Antimicrobial peptides (AMPs) of the innate immunity may play an important role in anti-infectious defense of the oral cavity, but their relative amount in saliva is low. It’s major component is Proline-rich peptides (PRPs), whose impact in antimicrobial protection remains poorly understood. We suggest that salivary PRPs may reveal their defensive functions upon interaction with other molecules, in particular with AMPs. The aim of this work is an investigation of the combined antibacterial action of salivary PRPs (fragments of Basic salivary proline-rich protein 1: P-H (37-51), IB6 (98-116), p1932) with antimicrobial peptides (histatin 5 and cathelicidin LL-37 and beta-defensin hBD3). Listed PRPs have been obtained by chemical solid-phase synthesis. The method of broth microdilutions was used to compare minimal inhibitory concentrations (MICs) of individual fractions of AMPs and their MICs in the presence of salivary peptides. It was found that in the presence of peptides IB6 (98-116) or P-H (37-51) the activity of defensin hBD3 was increased (reduction of MICs by 2 times) against Staphylococcus aureus SG511. In the presence of IB6 (98-116) or p1932 the activity of this defensin against E. coli ML35p was also improved (MICs of hBD3 was lowered by 2 times). For other combinations of the peptides, this effect was not observed. The obtained data confirm the assumption that the combined action of varied salivary peptides, including cationic Proline-rich peptides, plays an important role in anti-infectious protection of the oral cavity.

scholarly journals Royal Jelly Aliphatic Acids Contribute to Antimicrobial Activity of Honey

2018 ◽  
Vol 62 (1) ◽  
pp. 111-123 ◽  
Author(s):  
Walerij Isidorow ◽  
Stanisław Witkowski ◽  
Piotr Iwaniuk ◽  
Monika Zambrzycka ◽  
Izabela Swiecicka
Keyword(s):  
Fatty Acids ◽  
Antimicrobial Activity ◽  
Antibacterial Activity ◽  
Royal Jelly ◽  
Dicarboxylic Acids ◽  
Antibacterial Action ◽  
Larval Food ◽  
Nutrient Media ◽  
Minimal Inhibitory Concentrations ◽  
Aliphatic Acids

Abstract Honey is valued for its therapeutic qualities which are attributed among others to its antibacterial multifactorial properties. However, all the factors that influence these properties have not been identified. The present study is focused on the antibacterial action of fatty acids originating from royal jelly, the larval food of honeybees. Aliphatic C8-C12 acids characteristic of this bee product had previously been identified in more than fifty different samples of honey originating from seven countries and in eleven samples of Polish herbhoney. Experiments were performed to ascertain the influence of acidity on the antimicrobial activity of the acids. In acidic nutrient media all tested aliphatic hydroxyacids and unsaturated dicarboxylic acids demonstrated antibacterial action against different microbes with minimal inhibitory concentrations between 0.048 and 3.125 mM. Our results confirm that part of the antibacterial activity of honey contributes to these compounds of bee origin.

scholarly journals Identification of A Novel Antibacterial Peptide from Atlantic Mackerel belonging to the GAPDH-Related Antimicrobial Family and Its In Vitro Digestibility

Marine Drugs ◽  
2019 ◽  
Vol 17 (7) ◽  
pp. 413 ◽  
Author(s):  
Clément Offret ◽  
Ismaïl Fliss ◽  
Laurent Bazinet ◽  
André Marette ◽  
Lucie Beaulieu
Keyword(s):  
Antibacterial Activity ◽  
Solid Phase ◽  
Bioactive Molecules ◽  
Peptide Sequence ◽  
In Vitro Digestibility ◽  
Biotechnological Potential ◽  
Minimal Inhibitory Concentrations ◽  
Atlantic Mackerel ◽  
Gram Positive Bacteria

The Atlantic mackerel, Scomber scombrus, is one of the most fished species in the world, but it is still largely used for low-value products, such as bait; mainly for crustacean fishery. This resource could be transformed into products of high value and may offer new opportunities for the discovery of bioactive molecules. Mackerel hydrolysate was investigated to discover antibacterial peptides with biotechnological potential. The proteolytic process generated a hydrolysate composed of 96% proteinaceous compounds with molecular weight lower than 7 kDa. From the whole hydrolysate, antibacterial activity was detected against both Gram-negative and Gram-positive bacteria. After solid phase extraction, purification of the active fraction led to the identification of 4 peptide sequences by mass spectrometry. The peptide sequence N-KVEIVAINDPFIDL-C, called Atlantic Mackerel GAPDH-related peptide (AMGAP), was selected for chemical synthesis to confirm the antibacterial activity and to evaluate its stability through in vitro digestibility. Minimal inhibitory concentrations of AMGAP revealed that Listeria strains were the most sensitive, suggesting potential as food-preservative to prevent bacterial growth. In addition, in vitro digestibility experiments found rapid (after 20 min) and early digestibility (stomach). This study highlights the biotechnological potential of mackerel hydrolysate due to the presence of the antibacterial AMGAP peptide.

Salivary Histatin 5 and its Similarities to the Other Antimicrobial Proteins in Human Saliva

2000 ◽  
Vol 14 (1) ◽  
pp. 16-21 ◽  
Author(s):  
M. Edgerton ◽  
S.E. Koshlukova
Keyword(s):  
Antimicrobial Activity ◽  
Oral Cavity ◽  
Human Saliva ◽  
Oral Bacteria ◽  
Defense System ◽  
Antimicrobial Proteins ◽  
Cationic Proteins ◽  
Histatin 5 ◽  
Host Defense System ◽  
Bacteria And Fungi

Non-immune salivary proteins-including lactoperoxidase, lysozyme, lactoferrin, and histatins-are key components of the innate host defense system in the oral cavity. Many antimicrobial proteins contain multiple functional domains, with the result that one protein may have more than one mechanism of antimicrobial activity. These domains may be separated by proteolytic cleavage, creating smaller proteins with functional antimicrobial activity in saliva as described for lysozyme, lactoferrin, and histatins. These small cationic proteins then exert cytotoxic activity to oral bacteria and fungi. Salivary histatin 5 initiates killing of C. albicans through binding to yeast membrane proteins and non-lytic release of cellular ATP. Extracellular ATP may then activate fungal ATP receptors to induce ultimate cell death. This mechanism for fungal cytotoxicity may be shared by other antimicrobial cationic proteins. Microbicidal domains of salivary and host innate proteins should be considered as potential therapeutic agents in the oral cavity.

Synergy of action of antimicrobial peptides PG-1 and ChBac3.4 with antiseptics against antibiotic-resistant bacteria

2018 ◽  
Vol 18 (4) ◽  
pp. 47-57
Author(s):  
Maria Sergeyevna Zharkova ◽  
Ekaterina S. Umnyakova ◽  
Anna G. Afinogenova ◽  
Gennady E. Afinogenov ◽  
Aleksandr A. Kolobov ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Sodium Hypochlorite ◽  
Hemolytic Activity ◽  
Etidronic Acid ◽  
Resistant Bacteria ◽  
Bacterial Cells ◽  
Antibiotic Resistant Bacteria ◽  
Antibiotic Resistant ◽  
Bacterial Membranes ◽  
Combined Action

We investigated the combined effects of antimicrobial peptides PG-1 and ChBac3.4 with antiseptics (sodium hypochlorite, dioxidine, prontosan, poviargolum, and etidronic acid) to identify combinations that display synergistic antimicrobial activity against antibiotic-resistant bacteria. We used the checker-board titration method to calculate fractional inhibitory concentration indices, and based on the indices the type of combined action was determined. The combined effect on the metabolic activity of bacteria was evaluated using the fluorescent marker resazurin, and the effect on the permeability of bacterial membranes for chromogenic markers was studied spectrophotometrically. The combined hemolytic activity of the combinations was investigated. Sodium hypochlorite was shown to be antagonistic with both antimicrobial peptides. With other antiseptics, combined action was characterized by additivity or synergy. Synergy was most pronounced with the preparation of highly dispersed silver poviargolum. Antiseptics accelerate the development of the antimicrobial effect of antimicrobial peptides but do not significantly affect the dynamics of the membranolytic action of antimicrobial peptides on bacterial cells. Synergy of hemolytic activity is rare. Thus, the combined use of antimicrobial peptides and antiseptics is promising for combating antibiotic-resistant bacteria and can be used to reduce the toxic effects of these compounds.

scholarly journals Regulation of Fungal Infection by a Combination of Amphotericin B and Peptide 2, a Lactoferrin Peptide That Activates Neutrophils

2004 ◽  
Vol 11 (6) ◽  
pp. 1111-1119 ◽  
Author(s):  
Tetsuro Okamoto ◽  
Toyohiro Tanida ◽  
Benjuan Wei ◽  
Eisaku Ueta ◽  
Tetsuya Yamamoto ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Fungal Infection ◽  
Amphotericin B ◽  
Lethal Dose ◽  
Phosphatidyl Inositol ◽  
Antifungal Drugs ◽  
Histatin 5 ◽  
Gm Csf ◽  
Novel Strategy

ABSTRACT To establish a novel strategy for the control of fungal infection, we examined the antifungal and neutrophil-activating activities of antimicrobial peptides. The duration of survival of 50% of mice injected with a lethal dose of Candida albicans (5 × 108 cells) or Aspergillus fumigatus (1 × 108 cells) was prolonged 3 to 5 days by the injection of 10 μg of peptide 2 (a lactoferrin peptide) and 10 μg of α-defensin 1 for five consecutive days and was prolonged 5 to 13 days by the injection of 0.1 μg of granulocyte-monocyte colony-stimulating factor (GM-CSF) and 0.5 μg of amphotericin B. When mice received a combined injection of peptide 2 (10 μg/day) with amphotericin B (0.5 μg/day) for 5 days after the lethal fungal inoculation, their survival was greatly prolonged and some mice continued to live for more than 5 weeks, although the effective doses of peptide 2 for 50 and 100% suppression of Candida or Aspergillus colony formation were about one-third and one-half those of amphotericin B, respectively. In vitro, peptide 2 as well as GM-CSF increased the Candida and Aspergillus killing activities of neutrophils, but peptides such as α-defensin 1, β-defensin 2, and histatin 5 did not upregulate the killing activity. GM-CSF together with peptide 2 but not other peptides enhanced the production of superoxide (O2 −) by neutrophils. The upregulation by peptide 2 was confirmed by the activation of the O2 −-generating pathway, i.e., activation of large-molecule guanine binding protein, phosphatidyl-inositol 3-kinase, protein kinase C, and p47phox as well as p67phox. In conclusion, different from natural antimicrobial peptides, peptide 2 has a potent neutrophil-activating effect which could be advantageous for its clinical use in combination with antifungal drugs.

scholarly journals Heterologous Expression and Purification of the Antimicrobial Peptide Buforin II

2020 ◽  
Vol 0 (0) ◽  
Author(s):  
Boda Ferenc-András ◽  
Szabó Zoltán-István ◽  
Szőcs Erika ◽  
Salamon Pál ◽  
Orbán Csongor ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Heterologous Expression ◽  
Antimicrobial Peptide ◽  
Solid Phase ◽  
Host Cells ◽  
Fusion Partner ◽  
Monitoring And Control ◽  
Expression And Purification ◽  
Recombinant Peptide ◽  
Bacterial Membranes

AbstractAntimicrobial peptides are natural substances that have played a role in the development of the adaptive immune system, and are currently involved in the prevention of infections, through their direct antimicrobial and immunomodulatory properties. While the amino acid composition and spatial structure vary, most antibacterial peptides have a positive surface charge, which allows them to bind to the negative bacterial membranes. Buforin II is a widely studied antimicrobial peptide first obtained through the structural modification of buforin I, a peptide isolated from Bufo gargarizans. The peptide showed significant antibacterial activity against Gram-positive and Gram-negative bacterial strains. The mechanism of action of buforin II differs from that of other antimicrobial peptides, as it binds directly to bacterial DNA and RNA. The aim of our study was to obtain recombinant buforin II with a ubiquitin fusion partner, through heterologous expression in Escherichia coli Rosetta™ (DE3)pLysS cells, using a laboratory scale biore-actor. The incubation of expression host cells in a bioreactor allowed the constant monitoring and control of the process parameters, leading to high biomass levels and an increased production rate of the peptide. The parameters used during incubation were: 37°C, pH=6.9 and dissolved oxygen level above 40%. Purification of the recombinant protein was accomplished by affinity chromatography using a Ni-chelate solid phase to which the 10xHistag of our construct showed affinity. Method optimisation consisted in the use of gradient and linear elution, of which the latter was found to be more effective. Digestion of the fusion partner from the target peptide was performed with ubiquitin carboxyl-terminal hydrolase enzyme. The expression and purification protocols developed in our experiment allow the production of a significant amount of buforin II, allowing its use for further research. Furthermore, the presented methods could be suitable for industrial production of the recombinant peptide..

scholarly journals Antimicrobial Peptides Display Strong Synergy with Vancomycin Against Vancomycin-Resistant E. faecium, S. aureus, and Wild-Type E. coli

2020 ◽  
Vol 21 (13) ◽  
pp. 4578 ◽  
Author(s):  
Chih-Lung Wu ◽  
Ju-Yun Hsueh ◽  
Bak-Sau Yip ◽  
Ya-Han Chih ◽  
Kuang-Li Peng ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Synergistic Effects ◽  
Synergistic Activity ◽  
Wild Type ◽  
Bacterial Strains ◽  
Antibiotic Resistant ◽  
Minimal Inhibitory Concentrations ◽  
E Coli ◽  
Large Size ◽  
Vancomycin Resistant

There is an urgent and imminent need to develop new antimicrobials to fight against antibiotic-resistant bacterial and fungal strains. In this study, a checkerboard method was used to evaluate the synergistic effects of the antimicrobial peptide P-113 and its bulky non-nature amino acid substituted derivatives with vancomycin against vancomycin-resistant Enterococcus faecium, Staphylococcus aureus, and wild-type Escherichia coli. Boron-dipyrro-methene (BODIPY) labeled vancomycin was used to characterize the interactions between the peptides, vancomycin, and bacterial strains. Moreover, neutralization of antibiotic-induced releasing of lipopolysaccharide (LPS) from E. coli by the peptides was obtained. Among these peptides, Bip-P-113 demonstrated the best minimal inhibitory concentrations (MICs), antibiotics synergism, bacterial membrane permeabilization, and supernatant LPS neutralizing activities against the bacteria studied. These results could help in developing antimicrobial peptides that have synergistic activity with large size glycopeptides such as vancomycin in therapeutic applications.

scholarly journals Evaluation of the Antimicrobial Activity of Cationic Peptides Loaded in Surface-Modified Nanoliposomes against Foodborne Bacteria

2019 ◽  
Vol 20 (3) ◽  
pp. 680 ◽  
Author(s):  
Stefania Cantor ◽  
Lina Vargas ◽  
Oscar Rojas A. ◽  
Cristhian Yarce ◽  
Constain Salamanca ◽  
...  
Keyword(s):  
Antibacterial Activity ◽  
Light Scattering ◽  
Dynamic Light Scattering ◽  
Antimicrobial Peptides ◽  
Solid Phase ◽  
Peptide Sequence ◽  
Phase Method ◽  
Layer By Layer ◽  
Ethanol Injection ◽  
Hydrophilic Modification

Bacteria are a common group of foodborne pathogens presenting public health issues with a large economic burden for the food industry. Our work focused on a solution to this problem by evaluating antibiotic activity against two bacteria (Listeria monocytogenes and Escherichia coli) of relevance in the field of foodstuffs. We used two approaches: (i) structural modification of the antimicrobial peptides and (ii) nano-vehiculisation of the modified peptides into polymer-coated liposomes. To achieve this, two antimicrobial peptides, herein named ‘peptide +2′ and ‘peptide +5′ were synthesised using the solid phase method. The physicochemical characterisation of the peptides was carried out using measurements of surface tension and dynamic light scattering. Additionally, nanoliposomes were elaborated by the ethanol injection method and coated with a cationic polymer (Eudragit E-100) through the layer-by-layer process. Liposome characterisation, in terms of size, polydispersity and zeta potential, was undertaken using dynamic light scattering. The results show that the degree of hydrophilic modification in the peptide leads to different characteristics of amphipathicity and subsequently to different physicochemical behaviour. On the other hand, antibacterial activity against both bacteria was slightly altered after modifying peptide sequence. Nonetheless, after the encapsulation of the peptides into polymer-coated nano-liposomes, the antibacterial activity increased approximately 2000-fold against that of L. monocytogenes.

scholarly journals Candida albicans Mucin Msb2 Is a Broad-Range Protectant against Antimicrobial Peptides

2013 ◽  
Vol 57 (8) ◽  
pp. 3917-3922 ◽  
Author(s):  
Marc Swidergall ◽  
Andreas M. Ernst ◽  
Joachim F. Ernst
Keyword(s):  
Candida Albicans ◽  
Antimicrobial Peptides ◽  
Tight Binding ◽  
Surface Protein ◽  
Protective Effects ◽  
Content Type ◽  
Histatin 5 ◽  
Growth Environment ◽  
Corynebacterium Pseudodiphtheriticum ◽  
Lipopeptide Antibiotic

ABSTRACTThe human fungal pathogenCandida albicansreleases a large glycofragment of the Msb2 surface protein (Msb2*) into the growth environment, which protects against the action of human antimicrobial peptides (AMPs) LL-37 and histatin-5. Quantitation of Msb2*/LL-37 interactions by microscale thermophoresis revealed high-affinity binding (dissociation constant [KD] = 73 nM), which was lost or greatly diminished by lack ofO-glycosylation or by Msb2* denaturation. Msb2* also interacted with human α- and β-defensins and protectedC. albicansagainst these AMPs. In addition, the lipopeptide antibiotic daptomycin was bound and inactivated by Msb2*, which prevented the killing of bacterial pathogensStaphylococcus aureus,Enterococcus faecalis, andCorynebacterium pseudodiphtheriticum. In coculturings or mixed biofilms ofS. aureuswithC. albicanswild-type but notmsb2mutant strains, the protective effects of Msb2* on the bactericidal action of daptomycin were demonstrated. These results suggest that tight binding of shed Msb2* to AMPs that occurs during bacterial coinfections withC. albicanscompromises antibacterial therapy by inactivating a relevant reserve antibiotic.

A multi-walled carbon nanotube-based magnetic molecularly imprinted polymer as a highly selective sorbent for ultrasonic-assisted dispersive solid-phase microextraction of sotalol in biological fluids

The Analyst ◽  
2018 ◽  
Vol 143 (12) ◽  
pp. 2862-2875 ◽  
Author(s):  
Saeedeh Ansari ◽  
Saeed Masoum
Keyword(s):  
Carbon Nanotube ◽  
Molecularly Imprinted Polymer ◽  
Solid Phase Microextraction ◽  
Solid Phase ◽  
Biological Fluid ◽  
Biological Fluids ◽  
Imprinted Polymer ◽  
Molecularly Imprinted ◽  
Magnetic Molecularly Imprinted Polymer ◽  
Ultrasonic Assisted

A modified multiwalled carbon nanotube-based magnetic molecularly imprinted polymer (MWCNT-MMIP) was synthesized and applied for selective extraction and preconcentration of sotalol (SOT) in biological fluid samples by using ultrasonic-assisted dispersive solid-phase microextraction (UA-DSPME).

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