ENZYME-MEDIATED SELF-ASSEMBLY OF HIGHLY ORDERED STRUCTURES FROM DISORDERED PROTEINS

被引：0
|
作者：
Athamneh, Ahmad [1 ]
Barone, Justin [1 ]
机构：
[1] Virginia Tech, Dept Biol Syst Engn, Blacksburg, VA 24061 USA
来源：
SMASIS 2008: PROCEEDINGS OF THE ASME CONFERENCE ON SMART MATERIALS, ADAPTIVE STRUCTURES AND INTELLIGENT SYSTEMS - 2008, VOL 2 | 2009年
关键词：
AMYLOID-LIKE FIBRILS; OVALBUMIN;
D O I：
暂无
中图分类号：
TP [自动化技术、计算机技术];
学科分类号：
0812 ;
摘要：
Trypsin hydrolysis of wheat gluten produced glutamine-rich short peptides with a tendency to self-assemble into supermolecular structures extrinsic to native wheat gluten. Fourier transform infrared and X-ray diffraction data suggested that the new structures formed resembled that of cross-beta amyloid fibrils found in some insect silk and implicated in prion diseases. The superstructures were about 10 mu m in diameter with clear right-handed helical configuration and appeared to be bundles of smaller fibrils of about 63 nm in diameter. Results demonstrate the potential for utilizing cheap protein sources and natural mechanisms of protein self-assembly to design advanced nanomaterials that can provide a wide range of structural and chemical functionality.
引用
收藏
页码：625 / 628
页数：4
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