Sum-frequency spectroscopy and imaging of aligned helical polypeptides

被引:27
作者
Knoesen, A [1 ]
Pakalnis, S
Wang, M
Wise, WD
Lee, N
Frank, CW
机构
[1] Univ Calif Davis, Dept Elect & Comp Engn, Davis, CA 95616 USA
[2] Stanford Univ, Dept Chem Engn, Stanford, CA 94305 USA
基金
美国国家科学基金会;
关键词
biological materials; image generation; nonlinear optics; spectroscopy;
D O I
10.1109/JSTQE.2004.837226
中图分类号
TM [电工技术]; TN [电子技术、通信技术];
学科分类号
0808 ; 0809 ;
摘要
The sum-frequency spectroscopy signatures of NH-(amide A) and C = O (amide I) groups, the amide segments in all proteins, are measured in thin films that consist of an ensemble of right-handed, helical poly-gamma-benzyl-L-glutamate (PBLG) macromolecules that are endgrafted and self-organized into a monomolecular film with a large degree of unidirectional order. Distinct sum-frequency spectral signatures associated with the amide A and the amide I bands are observed because of a strong noncentro-symmetry produced by intra- and intermolecular forces. Hydrogen bonding self-organizes amino and acidic groups within the molecular helical scaffold. In an endgrafted thin film, repulsive electrostatic forces between PBLG macromolecules stabilize the organization between molecules. The average orientation of the PBLG chain was measured. Imaging scans using sum-frequency generation, complemented by atomic force microscopy, were used to investigate the uniformity of orientation of the PBLG chains.
引用
收藏
页码:1154 / 1163
页数:10
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