Sarkar Nandini, Kumar Manjeet, Dubey Vikash Kumar
Department of Biotechnology, Indian Institute of Technology Guwahati, Assam, India.
Biochim Biophys Acta. 2011 Sep;1810(9):809-14. doi: 10.1016/j.bbagen.2011.06.012. Epub 2011 Jun 24.
Deposition of protein fibrillar aggregates called amyloids in the tissue, is the principal cause of several degenerative diseases. Here, we have shown the disaggregation potential of rottlerin towards hen egg white lysozyme (HEWL) fibrils formed under alkaline conditions (pH-12.2).
Several biophysical methods like Atomic force microscopy (AFM), Fourier transform infrared spectroscopy (FTIR) and fluorescence emission spectra were used for the study.
Rottlerin exhibited instantaneous disaggregation effect on HEWL fibrils as monitored by Thioflavin T assay, anisotropy study and AFM imaging. Further we have monitored the conformational changes induced by rottlerin on the fibril in terms of surface hydrophobicity and secondary structure through 8-anilino-1-naphthalene sulfonic acid (ANS) fluorescence and FTIR study respectively. We have also attempted to elucidate the type of interaction between HEWL and rottlerin at pH-12.2 employing techniques like quenching study and FTIR.
Rottlerin seems to have potential application as anti-amyloid compound.
称为淀粉样蛋白的蛋白质纤维状聚集体在组织中的沉积是几种退行性疾病的主要原因。在此，我们展示了rottlerin对在碱性条件（pH - 12.2）下形成的鸡蛋清溶菌酶（HEWL）纤维的解聚潜力。
使用了几种生物物理方法，如原子力显微镜（AFM）、傅里叶变换红外光谱（FTIR）和荧光发射光谱进行研究。
通过硫黄素T测定、各向异性研究和AFM成像监测，rottlerin对HEWL纤维表现出即时解聚作用。此外，我们分别通过8 - 苯胺基 - 1 - 萘磺酸（ANS）荧光和FTIR研究，监测了rottlerin在表面疏水性和二级结构方面对纤维诱导的构象变化。我们还尝试采用猝灭研究和FTIR等技术，阐明在pH - 12.2条件下HEWL与rottlerin之间的相互作用类型。
rottlerin似乎具有作为抗淀粉样蛋白化合物的潜在应用。
