Abstract
Self-assembling peptides have shown tremendous potential in the fields of material sciences, nanoscience, and medicine. Because of the vast combinatorial space of even short peptides, identification of self-assembling sequences remains a challenge. Herein, we develop an experimental method to rapidly screen a huge array of peptide sequences for self-assembling property, using the one-bead one-compound (OBOC) combinatorial library method. In this approach, peptides on beads are N-terminally capped with nitro-1,2,3-benzoxadiazole, a hydrophobicity-sensitive fluorescence molecule. Beads displaying self-assembling peptides would fluoresce under aqueous environment. Using this approach, we identify eight pentapeptides, all of which are able to self-assemble into nanoparticles or nanofibers. Some of them are able to interact with and are taken up efficiently by HeLa cells. Intracellular distribution varied among these non-toxic peptidic nanoparticles. This simple screening strategy has enabled rapid identification of self-assembling peptides suitable for the development of nanostructures for various biomedical and material applications.
Highlights
Self-assembling peptides have shown tremendous potential in the fields of material sciences, nanoscience, and medicine
(1) Empirical design: most sequence design based on natural assembly peptides from biological systems such as KLVFF derived from parts of amyloid protein Aβ16–2019, and NFGAIL derived from a fragment of human islet amyloid polypeptide[20]
After side-chain deprotection, the beads were thoroughly washed with DMF, which was replaced stepwise with water or methanol and examined under a fluorescent microscope. Both (NBD)-KLVFF-beads and (NBD)-KAAGG-beads showed bright fluorescence. This is expected as the hydrophobicity-sensitive fluorescence dye NBD would fluoresce brightly under hydrophobic condition, in this case, methanol
Summary
Self-assembling peptides have shown tremendous potential in the fields of material sciences, nanoscience, and medicine. Similar to KLVFF, two other peptides (NFGAIL, LIVGD)[27] with known self-assembling properties were found to yield similar results, and were utilized as two additional positive controls (Supplementary Fig. 2). These results were gratifying as they demonstrated that such a simple assay would allow one to rapidly screen and identify self-assembling peptides from OBOC combinatorial libraries.
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