Mapping of Supramolecular Chirality in Insect Wings by Microscopic Vibrational Circular Dichroism Spectroscopy: Heterogeneity in Protein Distribution.
Hisako SatoAkihiko YamagishiMasaru ShimizuKeisuke WatanabeJun KoshoubuJun YoshidaIzuru KawamuraPublished in: The journal of physical chemistry letters (2021)
The supramolecular chirality of the hindwing of Anomala albopilosa (male) was investigated using a microscopic vibrational circular dichroism (VCD) system, denoted as MultiD-VCD. The source of intense infrared (IR) light for the system was a quantum cascade laser. Two-dimensional maps of IR and VCD spectra were taken by scanning the surface area (ca. 2 mm × 2 mm) of the insect hindwing tissue. The spectra ranged from 1500 to 1700 cm-1, and the maps have a spatial resolution of 100 μm. The distribution of proteins, including their supramolecular structures, was analyzed from the location-dependent spectral shape of the VCD bands assigned to amides I and II. The results revealed that the hindwing consists of segregated domains of proteins with different secondary structures: an α-helix (in one part of the membrane), a hybrid of α-helix and β-sheet (in another part of the membrane), and a coil (in a vein).
Keyphrases
- energy transfer
- high resolution
- density functional theory
- molecular dynamics
- single cell
- quantum dots
- single molecule
- water soluble
- high speed
- molecular dynamics simulations
- atomic force microscopy
- dna binding
- aedes aegypti
- transcription factor
- mass spectrometry
- protein protein
- magnetic resonance imaging
- binding protein
- magnetic resonance
- amino acid
- protein kinase
- small molecule