Gupta Veer Bala, Indi S S, Rao K S J
Department of Biochemistry and Nutrition, Central Food Technological Research Institute, Mysore, India.
J Mol Neurosci. 2008;34(1):35-43. doi: 10.1007/s12031-007-0070-z. Epub 2007 Sep 21.
Amyloid beta (Abeta) deposition and neurodegeneration are the two related events in the pathogenesis of Alzheimer's disease. Several factors modulate the conformation and physical properties of Abeta, which in turn affects its biological functions. Among these, age-dependent changes in the stereospecificity of the amino acids comprising Abeta is one such factors. In the present study, we investigated the aggregation property of Abeta as a function of the stereospecificity of amino acids comprising the peptide. We carried out our study by comparing the physical properties of Abeta(1-40) all-L and Abeta(1-40) all-D enantiomers using various biophysical techniques. These results indicated that the aggregation and folding parameters of Abeta are stereospecific and the aggregation property strongly depends upon the amino acid sequence and their stereospecificity. This may possibly help to understand the stereospecific role of amino acids comprising Abeta in its aggregation and its relevance to neurodegeneration.
淀粉样β蛋白（Aβ）沉积和神经退行性变是阿尔茨海默病发病机制中的两个相关事件。多种因素调节Aβ的构象和物理性质，进而影响其生物学功能。其中，构成Aβ的氨基酸立体特异性的年龄依赖性变化就是这样一个因素。在本研究中，我们研究了Aβ的聚集特性作为构成该肽的氨基酸立体特异性的函数。我们通过使用各种生物物理技术比较Aβ（1-40）全L型和Aβ（1-40）全D型对映体的物理性质来开展我们的研究。这些结果表明，Aβ的聚集和折叠参数具有立体特异性，并且聚集特性强烈依赖于氨基酸序列及其立体特异性。这可能有助于理解构成Aβ的氨基酸在其聚集中的立体特异性作用及其与神经退行性变的相关性。
