Unknown

Dataset Information

0

Directed surface attachment of nanomaterials via coiled-coil-driven self-assembly.


ABSTRACT: Numerous nanoscale devices and materials have been fabricated in recent years using a variety of biological scaffolds. However, the interfacing of these devices and materials into existing circuits and ordered arrays has proved problematic. Here, we describe a simple solution to this problem using self-assembly of the peptide coiled-coil heterodimer ACID:BASE to immobilize M13 bacteriophage particles to specific locations on a patterned gold surface. Surface plasmon resonance demonstrated that free ACID peptides will assemble onto a surface derivatized with BASE. We then displayed the ACID peptide on the pIX coat protein of M13 and showed that these phage particles permit formation of the coiled-coil resulting in specific surface attachment. The ACID:immobilized BASE affinities appear to be similar for free peptide and phage-displayed ACID. Finally, we fabricated two gold electrodes, separated by a 200 nm gap, coated one of them with BASE and showed that this allows localization of the M13:ACID onto the functionalized electrode.

SUBMITTER: White SJ 

PROVIDER: S-EPMC4785676 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

Directed surface attachment of nanomaterials via coiled-coil-driven self-assembly.

White Simon J SJ   Johnson Steven S   Szymonik Michal M   Wardingley Richard A RA   Pye Douglas D   Davies A Giles AG   Wälti Christoph C   Stockley Peter G PG  

Nanotechnology 20121116 49


Numerous nanoscale devices and materials have been fabricated in recent years using a variety of biological scaffolds. However, the interfacing of these devices and materials into existing circuits and ordered arrays has proved problematic. Here, we describe a simple solution to this problem using self-assembly of the peptide coiled-coil heterodimer ACID:BASE to immobilize M13 bacteriophage particles to specific locations on a patterned gold surface. Surface plasmon resonance demonstrated that f  ...[more]

Similar Datasets

| S-EPMC4744166 | biostudies-literature
| S-EPMC4570195 | biostudies-literature
| S-EPMC4756386 | biostudies-literature
| S-EPMC6760969 | biostudies-literature
| S-EPMC6355460 | biostudies-literature
| S-EPMC7878516 | biostudies-literature
| S-EPMC4433428 | biostudies-literature
| S-EPMC4744968 | biostudies-literature
| S-EPMC6449800 | biostudies-literature
| S-EPMC5084686 | biostudies-literature