Diphenylalanine peptide nanotubes self‐assembled on functionalized metal surfaces for potential application in drug‐eluting stent

Abstract

This study focuses on the potential of diphenylalanine self-assembled peptide nanotubes (FF Nts) for delivery of flufenamic acid (FA) from metal implants. Self-assembly of FF Nts was studied in solution and on surfaces of glass, silicone and gold substrates. FA was loaded inside the shell of FF Nts and subsequently FF/FA Nts were attached to gold surfaces. The substrate were characterized by Field Emission Scanning Electron Microscopy (FESEM), fluorescence microscopy, confocal microscopy, and UV-vis spectroscopy. Release of FA from FF Nts were investigated by immersing coated metal substrates in phosphate-buffered saline for 12 days. Self-assembly of FF in water and solvent resulted in formation of nanotubes, which efficiently loaded 98% of FA with concentration of 20 µg/mL. FESEM images confirmed successful attachment of FF/FA Nts to functionalized gold substrates. In vitro release studies indicated using FF Nts has prolonged the release rate of FA for several days. Biocompatibility studied confirmed more than 50% of the cells were alive in concentration of 250-1000 µg/mL of FF Nts thus suggesting the potential of peptide based self-assemble nanostructures as an alternate system for polymer coating in drugs eluting stents. © 2016 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 104A: 2280-2290, 2016.

Ultrashort Peptide Self-Assembly: Front-Runners to Transport Drug and Gene Cargos

“…The hydrophobic forces in these well-ordered tubular structures further facilitated to be soluble in a suitable solvent and self-assemble into well-organized films on various substrates. This technique was tried by Zohrabi et al (2016) wherein FFA loaded inside the H-Phe-Phe-OH nanotubes were coated onto Au surfaces functionalized with 3-mercaptopropionic acid (MPA). The biocompatibility and in vitro release studies confirmed the potential of H-Phe-Phe-OH nanotubes as an alternate system for polymer coating in drugs eluting stents.…”

Reductionist Approach in Peptide-Based Nanotechnology

“…The use of diphenylalanine for various technological applications has been repeatedly demonstrated (reviewed in 138). Such applications include providing energy for the locomotion of a nanoboat (140), production of electricity using a piezoelectric array of peptide nanorods (141) (Figure 2), coating of medical devices (142), and fabrication of a thermometer that measures low physiological temperatures (143) and those near absolute zero (144). For a list of some examples of technological applications and their references see Table 1.…”

Stackable Aromatic Dipeptide Ring Structures toward Nanotube Formation: Thermodynamics and Interactions in Gas‐Phase and Solution

“…[6][7][8][9][10] FFNTs have also been explored for use in the biomedical field as biomimetic scaffolds, sensors, and drug delivery agents due to their relatively nontoxic properties. [11][12][13] Building on these advancements, current studies are looking at other possible protein-like NTs that can be formed from modified FF, [14] l/d amino acids, [15][16][17] and dipeptides from the combination of other aromatic amino acids tryptophan (W) and tyrosine (Y). [18][19][20][21][22] The crystal structure of FFNTs has been well elucidated, [23][24][25][26][27] involving stacks of hexameric rings of FF in a head-to-tail conformation for intramolecular hydrogen bonding.…”

“…The early works of Reches and Gazit reported hollow self‐assembled FFNTs exhibiting exceptional stability and resistance from mechanical and chemical strains (e. g., heat, solvents, and enzymes), [4,5] leading to the development of FFNT with remarkable properties such as semi‐conductor properties, photoluminescence, imaging, nanofluidics, and quantum dots, to cite a few [6–10] . FFNTs have also been explored for use in the biomedical field as biomimetic scaffolds, sensors, and drug delivery agents due to their relatively nontoxic properties [11–13] . Building on these advancements, current studies are looking at other possible protein‐like NTs that can be formed from modified FF, [14] l/d amino acids, [15–17] and dipeptides from the combination of other aromatic amino acids tryptophan (W) and tyrosine (Y) [18–22] …”