Title

Fabrication of protein tubules: Immobilization of proteins on peptide tubules

Authors

Authors

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

Comments

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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

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