Structural Polymorphism of Lysozyme Amyloid Fibrils

Cholinium-Based Ionic Liquids Attenuate the Amyloid Fibril Formation of Lysozyme: A Greener Concept of Antiamyloidogenic Ionic Liquids

“…It can be well visualized from Figure a that the ellipticity (θ) values of these negative bands change from −55 (for native Lys) to −14 mdeg for the incubated solution of Lys. This implies that the structural integrity of Lys is disrupted by the formation of β-sheets, as the decrease in negative ellipticity accompanied by the peak shift reflects the formation of β-sheets, an observation that is well supported by the literature. ,, Through Figure c, it was perceived that when Lys was incubated under similar conditions of temperature and period in the presence of [Chn]­[Ac], the negative ellipticity increased as compared to Lys in fibrillar form (black line); however, there is a shift in peak (from 208 to 210 nm) as compared to native Lys. From Figure d, it is obvious that with [Chn]­[Bit] the CD analysis has not been fruitful as this particular IL, independent of the concentration, invariably shows a negative ellipticity peak near −200 .…”

“…To monitor the antiamyloidogenic action of [Chn] ILs for Lys fibrillation, the changes in the Lys structure were observed through CD spectroscopy. Under physiological conditions, Lys exhibits two negative bands at 208 and 222 nm characterizing the α+β class of the enzyme. , The far UV-CD spectra of native Lys and incubated Lys (at 65 °C and pH 2 for 6 days) in the absence and presence of various concentrations of [Chn] ILs are shown in Figure . It can be well visualized from Figure a that the ellipticity (θ) values of these negative bands change from −55 (for native Lys) to −14 mdeg for the incubated solution of Lys.…”