Self-assembling diphenylalanine peptide nanotubes selectively eradicate bacterial biofilm infection

Abstract

We outline, for the first time, the antibiofilm activity of diphenylalanine (FF) peptide nanotubes. Biofilm bacteria exhibit high tolerance to antimicrobials 10-10,000 times that of free-flowing planktonic forms. Biofilm infections are difficult to treat using conventional antimicrobial agents, leading to a rise in antimicrobial resistance. We discovered nanotubes composed of NH-FF-COOH demonstrated potent activity against staphylococcal biofilms implicated in hospital infections, resulting in complete kill at concentrations of 10 mg/mL. Carboxylic acid terminated FF nanotubes were able to destroy the exopolysaccharide architecture of staphylococcal biofilms expressing minimal toxicity, highlighting their potential for use in patients. Amidated (NH-FF-NH) forms demonstrated reduced antibiofilm efficacy and significant toxicity. These results contribute significantly to the development of innovative antibacterial technologies and peptide nanomaterials.

Halogen bonding as a key interaction in the self‐assembly of iodinated diphenylalanine peptides

“…Reches and Gazit reported the ability of diphenylalanine peptide to form well‐ordered nanotubes from aqueous solutions, and their application as molds for metal nanowires . From there, the scientific interest related to this peptide grew exponentially; indeed, recent research works showed the use of diphenylalanine for antibacterial agents, piezoelectric components for energy harvesters, optical waveguides, hydrogels, drug delivery systems, and integration of metal nanocomposites . Taking this aromatic dipeptide as elementary motif, many chemical modifications were investigated to control the morphology of the self‐assembled nano‐objects, tailoring the system for the desired application .…”

Surface Modification by Nano-Structures Reduces Viable Bacterial Biofilm in Aerobic and Anaerobic Environments

“…Molecular self-assembly has attracted extensive interest in the construction of antimicrobial and antifouling agents [ 13 , 14 , 15 , 16 , 17 , 18 , 19 , 20 , 21 , 22 , 23 , 24 ]. Self-assembly is a spontaneous process in which the molecular organization of diverse building blocks, including nucleic acids, peptides, proteins and lipids, organize into well-ordered structures at the nano-scale [ 25 , 26 , 27 , 28 ].…”

“…The underlying mechanism of this activity involves invasion into the bacterial cell followed by a reduction of glutathione levels [ 76 ]. The antibacterial properties of nano-assemblies formed by diphenylalanine have also been studied recently [ 19 , 20 ]. These assemblies cause membrane disruption in an E. coli model [ 20 ].…”

The Investigation of a Multi‐Functional Peptide as Gelator, Dyes Separation Agent and Metal Ions Adsorbent

“…Large numbers of peptide gels have been reported for the functions of tissue engineering, nanoreactors, drug delivery vehicle, antibacterial agent and regenerative medicine . Phenylalanine‐phenylalanine (FF) dipeptide is usually used as the core recognition of the β‐amyloid fiber and may be the simplest peptide with kinds of self‐assembled structures driven by the π‐π stacking interaction between the benzene rings . However, most of the peptides consisting of FF can hardly dissolve in water.…”