Báo cáo hóa học: " Aggregate structure of hydroxyproline-rich glycoprotein (HRGP) and HRGP assisted dispersion of carbon nanotubes"

Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành hóa học dành cho các bạn yêu hóa học tham khảo đề tài: bAggregate structure of hydroxyproline-rich glycoprotein (HRGP) and HRGP assisted dispersion of carbon nanotubes | Nanoscale Res Lett 2006 1 154-159 DOI s11671-006-9006-8 NANO EXPRESS Aggregate structure of hydroxyproline-rich glycoprotein HRGP and HRGP assisted dispersion of carbon nanotubes Ben Wegenhart Li Tan Michael Held Marcia Kieliszewski Liwei Chen Published online 1 August 2006 to the authors 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 gm 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 B. Wegenhart L. Tan M. Held M. Kieliszewski L. Chen H Department of Chemistry and Biochemistry Ohio University Athens Ohio 45701 USA e-mail chenl1@ of YK20 with retention of the extended polyproline-II

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