Posted by The interaction of a small, monomeric cytoplasmic protein, Cellular retinoic acid binding protein I (CRABPI), with cyclodextrins (α-, β-, and γ-CD) of different sizes was investigated.
γ-cyclodextrin has the highest binding affinity and stabilization effect. Enhancement of fluorescence intensity, lifetime, and secondary contents of protein with a decrease in structural fluctuations in in silico study strongly supports the outcome. β-CD shows moderate stabilizing behaviour, while α-CD engages primarily in superficial hydrogen bonding with minimal impact on protein conformation. It is significant to highlight that the large cavity size of γ-CD encapsulates the surface amino acids of CRABP I, supporting localized structural rigidification without disturbing the global fold of the protein.
Laxmipriya Prusty, Devi Prasanna Behera, Harekrushna Sahoo (2026) Cyclodextrin: A spectroscopic and in-silico investigation as a size-dependent cytoplasmic protein stabilizer. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 346, 126948.
https://doi.org/10.1016/j.saa.2025.126948.