Fabrication of protein tubules: Immobilization of proteins on peptide tubules

    Authors

    G. E. Douberly; S. Pan; D. Walters;H. Matsui

    Comments

    Authors: contact us about adding a copy of your work at STARS@ucf.edu

    Abbreviated Journal Title

    J. Phys. Chem. B

    Keywords

    DNA; NANOCRYSTALS; ORGANIZATION; ATTACHMENT; MONOLAYERS; MOLECULES; SURFACES; BIOTIN; AVIDIN; WIRES; Chemistry, Physical

    Abstract

    Peptide tubules, self-assemblies of bis(N-alpha -amido-glycylglycine)-1,7-heptane dicarboxylate, were functionalized by poly(L-lysine), D-biotin, avidin, and albumin bovine. Proteins were covalently immobilized on the peptide tubules via NHS ester intermediates, while amide groups of the peptide tubules were also capable of intercalating proteins via hydrogen bonds. These entities, tagged with fluorescein isothiocyanate, uniformly coated the peptide tubules as confirmed by fluorescence microscopy. Avidin coated the peptide tubules without denaturing, confirmed by fluorescein-tagged D-biotin attachment onto the avidin-coated peptide tubules, This result indicates that the protein tubules may be attached at desired surfaces using biological interactions such as antibody-antigen recognition. Such protein tubules may be used as building blocks for microdevice fabrication such as microelectronics and protein array biosensors.

    Journal Title

    Journal of Physical Chemistry B

    Volume

    105

    Issue/Number

    32

    Publication Date

    1-1-2001

    Document Type

    Article

    Language

    English

    First Page

    7612

    Last Page

    7618

    WOS Identifier

    WOS:000170494000004

    ISSN

    1089-5647

    Share

    COinS