Abstract
Peptide nanotubes are promising materials for a variety of biomedical applications with ultrashort (≤7 amino acids) forms providing particular promise for clinical translation. The manufacture of peptide nanotubes has, however, been associated with toxic organic solvents restricting clinical use. The purpose of this work is to formulate dipeptide nanotubes using mild techniques easily translated to industrial upscale and to characterize their physiochemical and biological properties. Phenylalanine-phenylalanine variants can be successfully formulated using distilled water as demonstrated here. Formulations are homogenous in shape (tubular), with apparent size (50-260 nm) and a zeta potential of up to +30 mV. L-(H2 N-FF-COOH), and D-enantiomers (H2 N-ff-COOH) demonstrate no toxicity against glioblastoma cells and are explored for ability to deliver a model hydrophilic molecule, sodium fluorescein, at pH 5.5 (tumor) and 7.4 (physiological). Peptide nanotubes loaded with >85% sodium fluorescein, demonstrate burst release characteristics, fitting the Weibull model of drug release. This research provides important data contributing to the pharmaceutical formulation of peptide nanotubes as drug delivery platforms for hydrophilic drugs.
Highlights
Peptide nanotubes are promising materials for a variety of biomedical applito certain “naked” drug molecules.[5,6] A cations with ultrashort (≤7 amino acids) forms providing particular promise for clinical translation
Peptide nanotubes are an exciting, innovative platform cur- as dipeptide nanotubes composed of two amino acid subunits, rently being researched for a variety of applications, including which are well documented for their ability to self-assemble.[15,16]
It has been widely established that the ability the body, ii) delivery of higher therapeutic drug concentrations, of a dipeptide motif to self-assemble into nanotube architeciii) passive targeting of nanoparticles to solid tumors through tures is largely dependent on the presence of two hydrophobic the enhanced permeability and retention effect, iv) permeation amino residues within the peptide primary sequence and the availability of hydrogen bonding.[17,18,19]
Summary
Peptide nanotubes are promising materials for a variety of biomedical applito certain “naked” drug molecules.[5,6] A cations with ultrashort (≤7 amino acids) forms providing particular promise for clinical translation. L-(H2N-FF-COOH), and D-enantiomers ical properties due to the varying nature of their amino acid R-chemical functional group This can be exploited, for example, to load a diverse array of molecules and drugs, including chemotherapies.[8,9,10]. Electronics,[1] sensors,[2] alternative energy harvesters,[3] and Utilizing the minimum number of subunits required to biomedical materials.[4] Nanoparticle formulations, including achieve self-assembly facilitates cheap manufacture thereby peptide nanotubes, can offer several unique advantages as increasing the potential for clinical translation and drug delivery platforms. Laverty for example a combination of π–π interactions, van der Waals
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
