Surface organization and nanopatterning of collagen by dip-pen nanolithography

被引:244
作者
Wilson, DL
Martin, R
Hong, S
Cronin-Golomb, M
Mirkin, CA
Kaplan, DL
机构
[1] Tufts Univ, Dept Chem & Biol Engn, Medford, MA 02155 USA
[2] Tufts Univ, Ctr Bioengn, Medford, MA 02155 USA
[3] Tufts Univ, Elect Engn & Comp Sci & Bioengn Ctr, Medford, MA 02155 USA
[4] Northwestern Univ, Dept Chem, Evanston, IL 60208 USA
关键词
D O I
10.1073/pnas.241323198
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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 anew strategy to study the important hierarchical assembly processes of biological systems.
引用
收藏
页码:13660 / 13664
页数:5
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