Surface organization and nanopatterning of collagen by dip-pen nanolithography

AUTOR(ES)

Wilson, Donna L.

FONTE

The National Academy of Sciences

RESUMO

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.

Documentos Relacionados

• Nucleotide Sequence of the Penicillinase Repressor Gene penI of Bacillus licheniformis and Regulation of penP and penI by the Repressor
• Nucleotide sequence of the penicillinase repressor gene penI of Bacillus licheniformis and regulation of penP and penI by the repressor.
• Number and organization of collagen genes in Caenorhabditis elegans.
• Effects of interferon-gamma on expression of cell surface receptors for collagen and deposition of newly synthesized collagen by cultured human lung fibroblasts.
• Radial organization of interstitial exchange pathway and influence of collagen in synovium.