4.8 Article

In Vitro Monitoring Conformational Changes of Polypeptide Monolayers Using Infrared Plasmonic Nanoantennas

期刊

NANO LETTERS
卷 19, 期 1, 页码 1-7

出版社

AMER CHEMICAL SOC
DOI: 10.1021/acs.nanolett.8b02372

关键词

Plasmonics; surface-enhanced infrared absorption spectroscopy; proteins; conformational changes; biosensing

资金

  1. ERC Advanced Grant (COMPLEXPLAS)
  2. Deutsche Forschungsgemeinschaft [SPP1391]
  3. Baden-Wurttemberg Stiftung (PROTEINSENS)
  4. MWK Baden-Wurttemberg (IQST)
  5. Max Planck Society
  6. BMBF [03IS2101E]
  7. Deutsche Forschungsgemeinschaft (DFG) [286735196]

向作者/读者索取更多资源

Proteins and peptides play a predominant role in biochemical reactions of living cells. In these complex environments, not only the constitution of the molecules but also their three-dimensional configuration defines their functionality. This so-called secondary structure of proteins is crucial for understanding their function in living matter. Misfolding, for example, is suspected as the cause of neurodegenerative diseases such as Alzheimer's and Parkinson's disease. Ultimately, it is necessary to study a single protein and its folding dynamics. Here, we report a first step in this direction, namely ultrasensitive detection and discrimination of in vitro polypeptide folding and unfolding processes using resonant plasmonic nanoantennas for surface enhanced vibrational spectroscopy. We utilize poly-L-lysine as a model system which has been functionalized on the gold surface. By in vitro infrared spectroscopy of a single molecular monolayer at the amide I vibrations we directly monitor the reversible conformational changes between alpha-helix and beta-sheet states induced by controlled external chemical stimuli. Our scheme in combination with advanced positioning of the peptides and proteins and more brilliant light sources is highly promising for ultrasensitive in vitro studies down to the single protein level.

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