All Stories

  1. Antimicrobial Peptides and their Multiple Effects at Sub-Inhibitory Concentrations
  2. Inorganic Gold and Polymeric Poly(Lactide-co-glycolide) Nanoparticles as Novel Strategies to Ameliorate the Biological Properties of Antimicrobial Peptides
  3. Nanotechnologies to Improve the Pharmacological Profile of Therapeutic Peptides
  4. The Potential of Frog Skin Peptides for Anti-Infective Therapies: The Case of Esculentin-1a(1-21)NH2
  5. Esculentin-1a Derived Antipseudomonal Peptides: Limited Induction of Resistance and Synergy with Aztreonam
  6. From liposomes to cells: Filling the gap between physicochemical and microbiological studies of the activity and selectivity of host-defense peptides
  7. Assessment of the potential of temporin peptides from the frog Rana temporaria (Ranidae) as anti-diabetic agents
  8. Esculentin-1a derived peptides kill Pseudomonas aeruginosa biofilm on soft contact lenses and retain antibacterial activity upon immobilization to the lens surface
  9. Cytotoxic peptides with insulin-releasing activities from skin secretions of the Italian stream frog Rana italica (Ranidae)
  10. Esculentin-1a-derived peptides promote clearance ofP. aeruginosainternalized in cystic fibrosis bronchial cells as well as lung cells migration: Biochemical properties and a plausible mode of action
  11. Antimicrobial peptides and wound healing: biological and therapeutic considerations
  12. Naturally Occurring Peptides from Rana temporaria: Antimicrobial Properties and More
  13. Editorial (Thematic Issue: Antimicrobial Peptides in Medicinal Chemistry: Advances and Applications)
  14. P‐113 Peptide: New experimental evidences on its biological activity and conformational insights from molecular dynamics simulations
  15. Temporins A and B Stimulate Migration of HaCaT Keratinocytes and Kill Intracellular Staphylococcus aureus
  16. A Lesson from Bombinins H, Mildly Cationic Diastereomeric Antimicrobial Peptides from Bombina Skin
  17. From frog integument to human skin: dermatological perspectives from frog skin biology
  18. Anti-Candida activity of 1–18 fragment of the frog skin peptide esculentin-1b: in vitro and in vivo studies in a Caenorhabditis elegans infection model
  19. NMR Structure of Temporin-1 Ta in Lipopolysaccharide Micelles: Mechanistic Insight into Inactivation by Outer Membrane
  20. Novel α-MSH Peptide Analogues with Broad Spectrum Antimicrobial Activity
  21. Esculentin(1-21), an amphibian skin membrane-active peptide with potent activity on both planktonic and biofilm cells of the bacterial pathogen Pseudomonas aeruginosa
  22. The effect of d-amino acid substitution on the selectivity of temporin L towards target cells: Identification of a potent anti-Candida peptide
  23. Bombinins
  24. Antioxidative and DNA Protective Effects of Bacillomycin D-Like Lipopeptides Produced by B38 Strain
  25. Isomerization of an Antimicrobial Peptide Broadens Antimicrobial Spectrum to Gram-Positive Bacterial Pathogens
  26. A Plausible Molecular Mechanism for the Synergistic Activity of Temporins at the Level of Lipopolysaccharide-Outer Membrane of Gram-Negative Bacteria
  27. Short Stories - on Antimicrobial Peptides that are Too Short to Span the Membrane
  28. Alteration of Local Microflora and α-defensins Hyper-production in Colonic Adenoma Mucosa
  29. Host-defense peptides: from biology to therapeutic strategies
  30. Short native antimicrobial peptides and engineered ultrashort lipopeptides: similarities and differences in cell specificities and modes of action
  31. Alanine scanning analysis and structure–function relationships of the frog‐skin antimicrobial peptide temporin‐1Ta
  32. Membrane interaction and antibacterial properties of two mildly cationic peptide diastereomers, bombinins H2 and H4, isolated from Bombina skin
  33. Structure−Activity Relationship, Conformational and Biological Studies of Temporin L Analogues
  34. Anti-Candida effect of bacillomycin D-like lipopeptides from Bacillus subtilis B38
  35. Triggering of the Antibacterial Activity of Bacillus subtilis B38 Strain against Methicillin-Resistant Staphylococcus aureus
  36. A new antibacterial and antioxidant S07-2 compound produced by Bacillus subtilis B38
  37. Effects of a Membrane-Active Amphibian Antimicrobial Peptide on the Bacterial Proteome
  38. Fluorescence and Electron Microscopy Methods for Exploring Antimicrobial Peptides Mode(s) of Action
  39. Esculentin‐1b(1–18) – a membrane‐active antimicrobial peptide that synergizes with antibiotics and modifies the expression level of a limited number of proteins in Escherichia coli
  40. Optimization of medium composition for the production of antimicrobial activity by Bacillus subtilis B38
  41. In vitro bactericidal activity of the N-terminal fragment of the frog peptide esculentin-1b (Esc 1–18) in combination with conventional antibiotics against Stenotrophomonas maltophilia
  42. Preface to Amphibian Antimicrobial Peptides
  43. Temporins and their synergism against Gram-negative bacteria and in lipopolysaccharide detoxification
  44. Esculentin 1–21: a linear antimicrobial peptide from frog skin with inhibitory effect on bovine mastitis‐causing bacteria
  45. Production of Anti-Methicillin-Resistant Staphylococcus Activity from Bacillus subtilis sp. Strain B38 Newly Isolated from Soil
  46. Folding propensity and biological activity of peptides: The effect of a single stereochemical isomerization on the conformational properties of bombinins in aqueous solution
  47. A Different Molecular Mechanism Underlying Antimicrobial and Hemolytic Actions of Temporins A and L
  48. Biological characterization and modes of action of temporins and bombinins H, multiple forms of short and mildly cationic anti‐microbial peptides from amphibian skin
  49. Effect of Natural l- to d-Amino Acid Conversion on the Organization, Membrane Binding, and Biological Function of the Antimicrobial Peptides Bombinins H
  50. Effects of the antimicrobial peptide temporin L on cell morphology, membrane permeability and viability of Escherichia coli
  51. An amphibian antimicrobial peptide variant expressed in Nicotiana tabacum confers resistance to phytopathogens
  52. Temporin L: antimicrobial, haemolytic and cytotoxic activities, and effects on membrane permeabilization in lipid vesicles
  53. Temporins, Antimicrobial Peptides from the European Red Frog Rana temporaria