A detailed analysis of the influence of β-cyclodextrin derivates on the thermal denaturation of lysozyme

摘要: Abstract The influence of HPβCD on the thermal denaturation lysozyme was analyzed mainly from microcalorimetry and Raman investigations carried out in molecular fingerprint low-frequency regions. It shown that spectroscopy performed a wide spectral range give opportunity to describe mechanism protein denaturation. Using D2O as solvent allowed us show destabilizes tertiary structure by enhancing flexibility thus inducing destabilization secondary structure. Principal components analysis (PCA) used for spectra treatment, providing important information about inclusion complex formation between hydrophobic residues CDs molecules. Combining PCA classical technics (curve fitting) data better understanding seems be related capacity form complex. observed these interactions prevent new strong H-bonds β-sheet structures thereby inhibiting aggregation. This study reveals are promising systems aggregation without denaturation, only if designing derivative is carefully controlled.