Understanding the adsorption of salmon calcitonin, antimicrobial peptide AP114 and polymyxin B onto lipid nanocapsules

Umerska, Anita; Matougui, Nada; Groo, Anne-Claire; Saulnier, Patrick

doi:10.1016/j.ijpharm.2016.04.028

Cited by 30 publications

(49 citation statements)

References 37 publications

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“…22 The adsorption efficiency (AE) and drug loading (DL) were calculated using the following equations:…”

Section: Characterization Of Lncsmentioning

confidence: 99%

“…22 Briefly, standard solutions of the APIs (0.1-1,000 µg/mL) were prepared in deionized water, and 20 µL of the standard or sample was injected into the SymmetryShield™ RP 18 5 µm 4.6×250 mm column (Waters, USA). A flow rate of 1.0 mL/min was employed using mobile phase A composed of 0.1% trifluoroacetic acid (TFA) in water and mobile phase B composed of 0.1% TFA in acetonitrile.…”

Section: Characterization Of Lncsmentioning

confidence: 99%

“…Instead, they are expected to be localized within or on the particle shell. 22 The adsorption of the peptide did not cause an important change in the properties of the LNCs ( Table 2). The size distribution remained unaffected, and the increase in the nanocapsule diameter, although statistically significant at the lowest LNC/peptide MMR, can be considered as negligible, because the difference in particle size was considerably small (1 nm).…”

mentioning

confidence: 91%

“…20,21 Our recent study showed that LNCs are capable of effectively adsorbing peptides, including AP114. 22 Recently, we proposed using fatty acids or monoglycerides as cosurfactants to obtain LNCs with antibacterial properties. 18 Monolaurin proved to be the most promising cosurfactant among all tested fatty acids and monoglycerides.…”

Section: Introductionmentioning

confidence: 99%

“…Such interaction is a multifactorial process that depends on the properties of both, the peptide and the nanocarrier, and also on experimental conditions such as concentration and the medium. 22,28 Both plectasin derivatives, AP114 and AP138, are peptides composed of 40 amino acids with very similar amino acid sequence and molecular weight ( Table 1). They differ only by 3 amino acids (positions 9, 17, and 26 from the amino end).…”

mentioning

confidence: 99%

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Synergistic interactions between antimicrobial peptides derived from plectasin and lipid nanocapsules containing monolaurin as a cosurfactant against <em>Staphylococcus aureus</em>

Umerska¹,

Cassisa²,

Bastiat³

et al. 2017

IJN

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Development of effective antibacterial agents for the treatment of infections caused by Gram-positive bacteria resistant to existing antibiotics, such as methicillin-resistant Staphylococcus aureus (MRSA), is an area of intensive research. In this work, the antibacterial efficacy of two antimicrobial peptides derived from plectasin, AP114 and AP138, used alone and in combination with monolaurin-lipid nanocapsules (ML-LNCs) was evaluated. Several interesting findings emerged from the present study. First, ML-LNCs and both plectasin derivatives showed potent activity against all 14 tested strains of S. aureus , independent of their resistance phenotype. Both peptides displayed a considerable adsorption (33%–62%) onto ML-LNCs without having an important impact on the particle properties such as size. The combinations of peptide with ML-LNC displayed synergistic effect against S. aureus , as confirmed by two methods: checkerboard and time-kill assays. This synergistic interaction enables a dose reduction and consequently decreases the risk of toxicity and has the potential of minimizing the development of resistance. Together, these results suggest that ML-LNCs loaded with a plectasin derivative may be a very promising drug delivery system for further development as a novel antibacterial agent against S. aureus , including MRSA.

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“…22 The adsorption efficiency (AE) and drug loading (DL) were calculated using the following equations:…”

Section: Characterization Of Lncsmentioning

confidence: 99%

Section: Characterization Of Lncsmentioning

confidence: 99%

mentioning

confidence: 91%

Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Synergistic interactions between antimicrobial peptides derived from plectasin and lipid nanocapsules containing monolaurin as a cosurfactant against <em>Staphylococcus aureus</em>

Umerska¹,

Cassisa²,

Bastiat³

et al. 2017

IJN

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Structural Biology of Calcitonin: From Aqueous Therapeutic Properties to Amyloid Aggregation

Kamgar-Parsi

Tolchard

Habenstein

et al. 2016

Israel Journal of Chemistry

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Under appropriate conditions, peptides and proteins can assemble from their native state into prefibrillar oligomers and then mature into fibrillar aggregates. This transition forms the molecular basis of several pathologies, often related to the deposition of these amyloid fibrils. Several hormone peptides involved in fundamental biological processes have the tendency to self‐assemble into amyloid fibrils, resulting in a loss of their native functions, and more importantly, entailing devastating consequences, such as the formation of amyloid depositions. Calcitonin is a 32 amino‐acid hormone peptide that can be considered a molecular paradigm for the central events associated with hormone misfolding. Calcitonin in its native form is involved in various physiological functions, including mediating calcium homeostasis and maintaining bone structure. It is the latter function that has motivated the use of calcitonin as an aqueous therapeutic agent for the treatment of bone‐related pathologies such as osteoporosis and Paget's disease. Despite some success as a therapeutic, calcitonin's ability to control these diseases is limited by its aggregation along the canonical amyloid aggregation pathway, compromising its long‐term stability as a therapeutic agent. A better understanding of the misfolding process would not only provide the structural basis to improve calcitonin's long‐term stability and activity as a therapeutic, but also provide valuable insights into pathological aggregation of other amyloids. In this work, we review the physiological roles of calcitonin, its structure, and aggregation process, and consider the effects of calcitonin's structure on its role as a therapeutic.

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Expression and characterization of the new antimicrobial peptide AP138L-arg26 anti Staphylococcus aureus

Zhang,

Yang,

Teng

et al. 2024

Appl Microbiol Biotechnol

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The low activity and yield of antimicrobial peptides (AMPs) are pressing problems. The improvement of activity and yield through modification and heterologous expression, a potential way to solve the problem, is a research hot-pot. In this work, a new plectasin-derived variant L-type AP138 (AP138L-arg26) was constructed for the study of recombination expression and druggablity. As a result, the total protein concentration of AP138L-arg26 was 3.1 mg/mL in Pichia pastoris X-33 supernatant after 5 days of induction expression in a 5-L fermenter. The recombinant peptide AP138L-arg26 has potential antibacterial activity against selected standard and clinical Gram-positive bacteria (G+, minimum inhibitory concentration (MIC) 2–16 µg/mL) and high stability under different conditions (temperature, pH, ion concentration) and 2 × MIC of AP138L-arg26 could rapidly kill Staphylococcus aureus (S. aureus) (> 99.99%) within 1.5 h. It showed a high safety in vivo and in vivo and a long post-antibiotic effect (PAE, 1.91 h) compared with vancomycin (1.2 h). Furthermore, the bactericidal mechanism was revealed from two dimensions related to its disruption of the cell membrane resulting in intracellular potassium leakage (2.5-fold higher than control), and an increase in intracellular adenosine triphosphate (ATP), and reactive oxygen species (ROS), the decrease of lactate dehydrogenase (LDH) and further intervening metabolism in S. aureus. These results indicate that AP138L-arg26 as a new peptide candidate could be used for more in-depth development in the future. Key points • The AP138L-arg26 was expressed in the P. pastoris expression system with high yield • The AP138 L-arg26 showed high stability and safety in vitro and in vivo • The AP138L-arg26 killed S. aureus by affecting cell membranes and metabolism

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Understanding the adsorption of salmon calcitonin, antimicrobial peptide AP114 and polymyxin B onto lipid nanocapsules

Cited by 30 publications

References 37 publications

Synergistic interactions between antimicrobial peptides derived from plectasin and lipid nanocapsules containing monolaurin as a cosurfactant against <em>Staphylococcus aureus</em>

Synergistic interactions between antimicrobial peptides derived from plectasin and lipid nanocapsules containing monolaurin as a cosurfactant against <em>Staphylococcus aureus</em>

Structural Biology of Calcitonin: From Aqueous Therapeutic Properties to Amyloid Aggregation

Expression and characterization of the new antimicrobial peptide AP138L-arg26 anti Staphylococcus aureus

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