Nanospectroscopy of single purple membranes by mid-IR resonantly-enhanced mechanical photoexpansion

Giliberti, Valeria; Badioli, Michela; Baldassarre, Leonetta; Nucara, A.; Calvani, P.; Ritter, Eglof; Puškar, Ljiljana; Hegemann, Peter; Schade, U.; Ortolani, Michele

doi:10.1117/12.2253851

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Afm-ir1

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2017

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“…This technique is now recognized as resonance enhanced AFM-IR (RE-AFM-IR) and significantly improves the sensitivity compared to the original AFM-IR technique. Using RE-AFM-IR, several research groups have demonstrated nanoscale IR imaging of polymers − and biomembranes − with sensitivity down to monolayers. Benefiting from the improved sensitivity, time-resolved RE-AFM-IR experiments, monitoring the structural changes in poly- l -lysine, have been performed with a temporal resolution of 15 s per spectrum over a spectral range of more than 100 cm –1 .…”

Section: Afm-irmentioning

confidence: 99%

Spectroscopic Imaging at the Nanoscale: Technologies and Recent Applications

Xiao

Schultz

2017

Anal. Chem.

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Section: Afm-irmentioning

confidence: 99%

Spectroscopic Imaging at the Nanoscale: Technologies and Recent Applications

Xiao

Schultz

2017

Anal. Chem.

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Heterogeneity of the Transmembrane Protein Conformation in Purple Membranes Identified by Infrared Nanospectroscopy

Giliberti

Badioli

Nucara

et al. 2017

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Cell membranes are intrinsically heterogeneous, as the local protein and lipid distribution is critical to physiological processes. Even in template systems embedding a single protein type, like purple membranes, there can be a different local response to external stimuli or environmental factors, resulting in heterogeneous conformational changes. Despite the dramatic advances of microspectroscopy techniques, the identification of the conformation heterogeneity is still a challenging task. Tip-enhanced infrared nanospectroscopy is here used to identify conformational changes connected to the hydration state of the transmembrane proteins contained in a 50 nm diameter cell membrane area, without the need for fluorescent labels. In dried purple membrane monolayers, areas with fully hydrated proteins are found among large numbers of molecules with randomly distributed hydration states. Infrared nanospectroscopy results are compared to the spectra obtained with diffraction-limited infrared techniques based on the use of synchrotron radiation, in which the diffraction limit still prevents the observation of nanoscale heterogeneity.

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Nanospectroscopy of single purple membranes by mid-IR resonantly-enhanced mechanical photoexpansion

Cited by 2 publications

References 18 publications

Spectroscopic Imaging at the Nanoscale: Technologies and Recent Applications

Spectroscopic Imaging at the Nanoscale: Technologies and Recent Applications

Heterogeneity of the Transmembrane Protein Conformation in Purple Membranes Identified by Infrared Nanospectroscopy

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