Germanium Plasmon Enhanced Resonators for Label-Free Terahertz Protein Sensing

被引：5

作者：

Bettenhausen, Maximilian ^{[1
,2
]}

Roemer, Friedhard ^{[1
,2
]}

Witzigmann, Bernd ^{[1
,2
]}

Flesch, Julia ^{[3
]}

Kurre, Rainer ^{[3
]}

Korneev, Sergej ^{[3
]}

Piehler, Jacob ^{[3
]}

You, Changjiang ^{[3
]}

Kazmierczak, Marcin ^{[4
]}

Guha, Subhajit ^{[4
]}

Capellini, Giovanni ^{[4
]}

Schroeder, Thomas ^{[4
]}

机构：

[1] Univ Kassel, Elect Engn Comp Sci Dept, Kassel, Germany

[2] Univ Kassel, CINSaT, Kassel, Germany

[3] Univ Osnabruck, Dept Biol Chem, Osnabruck, Germany

[4] IHP, Frankfurt, Oder, Germany

来源：

FREQUENZ | 2018年 / 72卷 / 3-4期

关键词：

terahertz sensor; protein conformation; semiconductor plasmonics; DIFFERENCE SPECTROSCOPY; ABSORPTION-SPECTROSCOPY; SURFACE; MONOLAYERS; MEMBRANE; DYNAMICS; IMMOBILIZATION; NANOPARTICLES; PASSIVATION; BIOSENSOR;

D O I：

10.1515/freq-2018-0009

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：

A Terahertz protein sensing concept based on subwavelength Ge resonators is presented. Ge bowtie resonators, compatible with CMOS fabrication technology, have been designed and characterized with a resonance frequency of 0.5 THz and calculated local intensity enhancement of 10.000. Selective biofunctionalization of Ge resonators on Si wafer was achieved in one step using lipoic acid-HaloTag ligand (LA-HTL) for biofunctionalization and passivation. The results lay the foundation for future investigation of protein tertiary structure and the dynamics of protein hydration shell in response to protein conformation changes.

引用

页码：113 / 122

页数：10

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