Chiroptical spectroscopy exploring the interaction of matter with polarized light provides many tools for molecular structure and interaction studies. Here, some recent discoveries are reviewed, primarily in the field of vibrational optical activity. Technological advances results in the development of more sensitive vibrational circular dichroism (VCD), Raman optical activity (ROA) or circular polarized luminescence (CPL) spectrometers. Significant contributions to the field also come from the light scattering and electronic structure theories, and their implementation in computer systems. Finally, new chiroptical phenomena have been observed, such as enhanced circular dichroism of biopolymers (protein fibrils, nucleic acids), plasmonic and resonance chirality‐transfer ROA experiments. Some of them are not yet understood or attributed to instrumental artifacts so far. Nevertheless, these unknown territories also indicate the vast potential of the chiroptical spectroscopy, and their investigation is even more challenging.

Protein fibrils are involved in a number of biological processes. Because their structure is very complex and not completely understood, different spectroscopic methods are used to monitor different aspects of fibril structure. We have explored circularly polarized luminescence (CPL) induced in lanthanide compounds to indicate fibril growth and discriminate among fibril types. For hen egg-white lysozyme and polyglutamic acid-specific CPL, spectral patterns were obtained and could be correlated with vibrational circular dichroism (VCD) spectra and thioflavin T fluorescence. The CPL spectra were measured on a Raman optical activity spectrometer, and its various polarization modes are discussed. The experiments indicate that the induced CPL is sensitive to more local aspects of the fibril structure than VCD. For CPL, smaller amounts of the sample are required for the analysis, and thus this method appears to be a good candidate for future spectroscopic characterization of these peptide and protein aggregates.

Vibrational circular dichroism (VCD) spectroscopy has been widely used to study (bio)molecules in solution. However, its solid-state applications have been restricted due to experimental limitations and artifacts. Having overcome some of them, the first VCD study of nucleoside crystals is now presented. A two-orders-of-magnitude enhancement of VCD signal was observed due to high molecular order in the crystals and resulting supramolecular chirality. This allowed to obtain high-quality VCD spectra within minutes using minute amounts of samples. The VCD technique is extremely sensitive in detecting changes in a crystal order and is able to distinguish different hydration states of crystals. This elevates it to a new level, as a fast and efficient tool to study chiral crystalline samples. This study demonstrates that VCD is capable of near-instantaneous detection of hydration polymorphs and crystal degradation, which is of substantial interest in pharmaceutical industry (quality and stability control).