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Proc Natl Acad Sci U S A. 2001 Nov 20;98(24):13660-4. Epub 2001 Nov 13.

Surface organization and nanopatterning of collagen by dip-pen nanolithography.

Author information

1
Department of Chemical and Biological Engineering and Bioengineering Center, Tufts University, Medford, MA 02155, USA.

Abstract

Collagen is a key fibrous protein in biological systems, characterized by a complex structural hierarchy as well as the ability to self-assemble into liquid crystalline mesophases. The structural features of collagen influence cellular responses and material properties, with importance for a wide range of biomaterials and tissue architectures. The mechanism by which fibrillar collagen structures form from liquid crystalline mesophases is not well characterized. We report positive printing of collagen and a collagen-like peptide down to 30-50-nm line widths, using the atomic force microscopy technique of dip-pen nanolithography. The method preserved the triple-helical structure and biological activity of collagen and even fostered the formation of characteristic higher levels of structural organization. The "direct-write" capability of biologically relevant molecules, while preserving their structure and functionality, provides tremendous flexibility in future biological device applications and in proteomics arrays, as well as a new strategy to study the important hierarchical assembly processes of biological systems.

PMID:
11707577
PMCID:
PMC61097
DOI:
10.1073/pnas.241323198
[Indexed for MEDLINE]
Free PMC Article

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