Monitoring protein configurations in the fingerprint region with micro-FTIR spectroscopy by employing a 98 fs solid-state laser tunable from 1.33 to 8 µm at 73 MHz repetition rate (Conference Presentation)

Florian Mörz; Rostyslav Semenyshyn; Frank Neubrech; Tobias Steinle; Andy Steinmann; Harald Giessen

doi:10.1117/12.2287176

14 March 2018 Monitoring protein configurations in the fingerprint region with micro-FTIR spectroscopy by employing a 98 fs solid-state laser tunable from 1.33 to 8 µm at 73 MHz repetition rate (Conference Presentation)

Florian Mörz, Rostyslav Semenyshyn, Frank Neubrech, Tobias Steinle, Andy Steinmann, Harald Giessen

Author Affiliations +

Proceedings Volume 10522, Frontiers in Ultrafast Optics: Biomedical, Scientific, and Industrial Applications XVIII; 1052202 (2018) https://doi.org/10.1117/12.2287176
Event: SPIE LASE, 2018, San Francisco, California, United States

Abstract

We monitor the configuration of poly-L-lysine proteins using vibrational resonances at 6 µm (1667 cm^-1) by employing a broadband femtosecond solid-state laser for micro-FTIR spectroscopy. This laser system allows for detection of minute amounts of proteins due to a several orders of magnitude higher brilliance compared to standard FTIR light sources such as globars. Thus, absorption signals as small as 0.5% can be detected without averaging, compared to 6.4% using a globar, at a spatial resolution as small as 10x10 µm^2. Our light source is based on a 98 fs, Yb-doped pump laser at 73 MHz repetition rate, providing 2.5 W average power. By pumping a fiber-feedback optical parametric oscillator (ffOPO) and a post-amplifier, signal and idler beams spanning from 1.33 – 2.0 and 2.1 – 4.6 µm are generated. The tuning range is extended to 8 µm by difference frequency generation between the signal and idler beams and can be further extended by using a pump laser with higher output power. At 7 µm excellent long-term wavelength stability with fluctuations smaller than 0.1% rms measured over 9 hours is observed, without applying electronic stabilization. This is due to the combination of a ffOPO with a post-amplifier and is distinctly superior over other systems based on free-space OPOs. Protein sensing is conducted by applying resonant surface-enhanced infrared absorption (SEIRA) spectroscopy, using a single gold nanoantenna. To the best of our knowledge, this is the first demonstration of resonant SEIRA spectroscopy using a single nanoantenna with a laser system as light source.

Conference Presentation

Citation Download Citation

Florian Mörz, Rostyslav Semenyshyn, Frank Neubrech, Tobias Steinle, Andy Steinmann, and Harald Giessen "Monitoring protein configurations in the fingerprint region with micro-FTIR spectroscopy by employing a 98 fs solid-state laser tunable from 1.33 to 8 µm at 73 MHz repetition rate (Conference Presentation)", Proc. SPIE 10522, Frontiers in Ultrafast Optics: Biomedical, Scientific, and Industrial Applications XVIII, 1052202 (14 March 2018); https://doi.org/10.1117/12.2287176

ACCESS THE FULL ARTICLE

INSTITUTIONAL
Select your institution to access the SPIE Digital Library.

SELECT YOUR INSTITUTION

PERSONAL
Sign in with your SPIE account to access your personal subscriptions or to use specific features such as save to my library, sign up for alerts, save searches, etc.

PERSONAL SIGN IN

No SPIE Account? Create one

PURCHASE THIS CONTENT

SUBSCRIBE TO DIGITAL LIBRARY

50 downloads per 1-year subscription

Members: $195

Non-members: $335 ADD TO CART

25 downloads per 1 - year subscription

Members: $145

Non-members: $250 ADD TO CART

PURCHASE SINGLE ARTICLE

Includes PDF, HTML & Video, when available

Members: $17.00

Non-members: $21.00 ADD TO CART

PROCEEDINGS
PRESENTATION

WATCH
PRESENTATION SAVE TO MY LIBRARY

GET CITATION

KEYWORDS

Spectroscopy

Infrared spectroscopy

Proteins

Laser systems engineering

Absorption spectroscopy

Absorption

Infrared radiation

Show All Keywords

Keywords/Phrases

Search In:

Publication Years