Peptide Self-Assembled Nanostructures with Distinct Morphologies and Properties Fabricated by Molecular Design

Meiwen Cao, Sha Lu, Wenjing Zhao, Li Deng, Meng Wang, Jiqian Wang, Peng Zhou, Dong Wang, Hai Xu, Jian R. Lu

    Research output: Contribution to journalArticlepeer-review

    Abstract

    Six surfactant-like peptides with the same amino acid composition but different primary sequences are designed, including G3A3V3I3K3, K3I3V3A3G3, I3V3A3G3K3, K3G3A3V3I3, V3G3I3A3K3, and K3A3I3G3V3. These peptides form antiparallel β-sheets during self-assembly. Because the constituent residues have different side chain size and hydrophobicity, sequence changes adjust group distribution and hydrophobicity on the two sides of a given β-sheet. This consequently tunes the binding energy of the side-to-side pairing conformations and leads to different self-assembled structures. G3A3V3I3K3 and K3I3V3A3G3 form short nanorods with diameters of 8.5 ± 1.0 nm and lengths <150 nm. I3V3A3G3K3 and K3G3A3V3I3 form nanosheets with heights of 4.0 ± 0.5 nm and limited lengths and widths. V3G3I3A3K3 and K3A3I3G3V3 form long fibrils with diameters of 7.0 ± 1.0 nm and lengths of micrometer scale. These nanostructures exhibit different capacity in encapsulating insoluble hydrophobic drug molecules and delivering them into the cells. The nanosheets of I3V3A3G3K3 and K3G3A3V3I3 can encapsulate both nile red and doxorubicin molecules to an extent of up to 17-23% in mole ratio. Moreover, the shape and size of the nanostructures affect the drug delivery into cells greatly, with the nanosheets and short rods exhibiting higher efficiency than the long fibrils. The study provides new insights into programmed peptide self-assembly toward specific functionalities.

    Original languageEnglish
    Pages (from-to)39174-39184
    Number of pages11
    JournalACS Applied Materials and Interfaces
    Volume9
    Issue number45
    Early online date25 Oct 2017
    DOIs
    Publication statusPublished - 2017

    Keywords

    • drug delivery
    • encapsulation
    • nanostructures
    • peptide self-assembly
    • primary sequence
    • β-sheet pairing

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