材料科学
酶
自组装
化学
结晶学
纳米技术
生物化学
作者
Ahmad I. M. Athamneh,Justin R. Barone
标识
DOI:10.1088/0964-1726/18/10/104024
摘要
Wheat gluten is an amorphous storage protein. Trypsin hydrolysis of wheat gluten produced glutamine-rich peptides. Some peptides were able to self-assemble into fibrous structures extrinsic to native wheat gluten. The final material was an in situ formed peptide composite of highly ordered nanometer-sized fibrils and micron-sized fibers embedded in an unassembled peptide matrix. Fourier transform infrared spectroscopic and x-ray diffraction data suggested that the new structures resembled that of cross- ? fibrils found in some insect silk and implicated in prion diseases. The largest self-assembled fibers were about 10??m in diameter with right-handed helicity and appeared to be bundles of smaller nanometer-sized fibrils. Results demonstrated the potential for utilizing natural mechanisms of protein self-assembly to design advanced materials that can provide a wide range of structural and chemical functionality.
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