Aggregate structure of hydroxyproline-rich glycoprotein (HRGP) and HRGP assisted dispersion of carbon nanotubes

  • Ben Wegenhart1,

    Affiliated with

    • Li Tan1,

      Affiliated with

      • Michael Held1,

        Affiliated with

        • Marcia Kieliszewski1 and

          Affiliated with

          • Liwei Chen1Email author

            Affiliated with

            Nanoscale Research Letters20061:154

            DOI: 10.1007/s11671-006-9006-8

            Published: 1 August 2006

            Abstract

            Hydroxyproline-rich glycoproteins (HRGP) comprise a super-family of extracellular structural glycoproteins whose precise roles in plant cell wall assembly and functioning remain to be elucidated. However, their extended structure and repetitive block co-polymer character of HRGPs may mediate their self-assembly as wall scaffolds by like-with-like alignment of their hydrophobic peptide and hydrophilic glycopeptide modules. Intermolecular crosslinking further stabilizes the scaffold. Thus the design of HRGP-based scaffolds may have practical applications in bionanotechnology and medicine. As a first step, we have used single-molecule or single-aggregate atomic force microscopy (AFM) to visualize the structure of YK20, an amphiphilic HRGP comprised entirely of 20 tandem repeats of: Ser-Hyp4-Ser-Hyp-Ser-Hyp4-Tyr-Tyr-Tyr-Lys. YK20 formed tightly aggregated coils at low ionic strength, but networks of entangled chains with a porosity of ~0.5–3 μm at higher ionic strength. As a second step we have begun to design HRGP-carbon nanotube composites. Single-walled carbon nanotubes (SWNTs) can be considered as seamless cylinders rolled up from graphene sheets. These unique all-carbon structures have extraordinary aromatic and hydrophobic properties and form aggregated bundles due to strong inter-tube van der Waals interactions. Sonicating aggregated SWNT bundles with aqueous YK20 solubilized them presumably by interaction with the repetitive, hydrophobic, Tyr-rich peptide modules of YK20 with retention of the extended polyproline-II character. This may allow YK20 to form extended structures that could potentially be used as scaffolds for site-directed assembly of nanomaterials.

            Keywords

            Hydroxyproline-rich glycoprotein Carbon nanotube Nano assembly

            [126]

            Declarations

            Acknowledgments

            B. W. thanks the Ohio Univeristy PACE (Program to Aid Career Exploration) for financial support. This project was supported by grants from the Ohio University NanobioTechnology Initiative (NBTI), the Herman Frasch Foundation (526-HF02), and the United States Department of Agriculture (2004–34490–14579).

            Authors’ Affiliations

            (1)
            Department of Chemistry and Biochemistry, Ohio University

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            © to the authors 2006