Fabrication of protein tubules: Immobilization of proteins on peptide tubules

Citation
Ge. Douberly et al., Fabrication of protein tubules: Immobilization of proteins on peptide tubules, J PHYS CH B, 105(32), 2001, pp. 7612-7618
Citations number
23
Categorie Soggetti
Physical Chemistry/Chemical Physics
Journal title
JOURNAL OF PHYSICAL CHEMISTRY B
ISSN journal
15206106 → ACNP
Volume
105
Issue
32
Year of publication
2001
Pages
7612 - 7618
Database
ISI
SICI code
1520-6106(20010816)105:32<7612:FOPTIO>2.0.ZU;2-S
Abstract
Peptide tubules, self-assemblies of bis(N-alpha -amido-glycylglycine)-1,7-h eptane dicarboxylate, were functionalized by poly(L-lysine), D-biotin, avid in, and albumin bovine. Proteins were covalently immobilized on the peptide tubules via NHS ester intermediates, while amide groups of the peptide tub ules were also capable of intercalating proteins via hydrogen bonds. These entities, tagged with fluorescein isothiocyanate, uniformly coated the pept ide tubules as confirmed by fluorescence microscopy. Avidin coated the pept ide tubules without denaturing, confirmed by fluorescein-tagged D-biotin at tachment onto the avidin-coated peptide tubules, This result indicates that the protein tubules may be attached at desired surfaces using biological i nteractions such as antibody-antigen recognition. Such protein tubules may be used as building blocks for microdevice fabrication such as microelectro nics and protein array biosensors.