Surface-Enhanced Infrared Absorption Microscopy for protein structural analysis

FTIR spectroscopy has been used extensively for the determination of secondary structure elements of proteins. However, it has always suffered from sensitivity limits (hundreds of μM) and the strong interference from water signals. The optimization of fluidic devices based on plasmonic nanosresonators in the IR regime allowed di overcome the former limitation. It is nowadays well-established that Surface-Enhanced Infrared Absorption (SEIRA) in plasmonic internal reflection (PIR) geometry is a very informative tool for the study of protein secondary structure. 

PIR-SEIRA performances have been proven for assesing the very subtle secondary structure modifications associated with the binding of Lapatinib, a tyrosine kinase inhibitor (TKI), to epidermal growth factor receptor (EGFR), a well-known driver of tumorigenesis in pathological settings such as lung, breast and brain cancers, as well as for the study of the dimerization of the SARS CoV-2 main protease, Mpro.

Retrieve Articles

Binding of tyrosine kinase inhibitor to epidermal growth factor receptor: surface-enhanced infrared absorption microscopy reveals subtle protein secondary structure variations.
Paolo Zucchiatti, Giovanni Birarda, Andrea Cerea, Marta S. Semrau, Aliaksandr Hubarevich, Paola Storici, Francesco De Angelis, Andrea Toma, Lisa Vaccar

Nanoscale 13(16), 7667-7677 (2021)

Dimeric and monomeric conformation of SARS-CoV-2 main protease: New technical approaches based on IR radiation.
Federica Piccirilli, Hendrik Vondracek, Lucia Silvestrini, Pietro Parisse, Francesco Spinozzi, Lisa Vaccari, et al.
Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 322, 124772 (2024)