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对阿波利波蛋白B-100的α-2域进行计算分析,这是LDL聚合的潜在触发因素

Joanne Jennifer E Tan¹, Marvin M Bilog², Adam A Profit²

¹Department of Biochemistry and Molecular Biology, College of Medicine, University of the Philippines Manila, Ermita, Manila 1000, Philippines.

Biochimica et biophysica acta. General subjects

|December 16, 2024

概括

电子阴性LDL,或LDL(-),由于错误折叠的阿波利波蛋白B-100而与粉样蛋白类似的聚合物. 来自apo B-100 α2域的特定,特别是螺旋 p,显示出显著的氨基原性质,可能触发动脉硬化中的LDL聚合.

科学领域:

生物化学生物化学
分子生物学分子生物学
心血管研究研究心血管研究

背景情况:

动脉样硬化与低密度脂蛋白 (LDL) 在动脉中的积累有关.
电子阴性LDL (LDL(-)) 呈现出类似于粉样蛋白的聚合.
在LDL中错误折叠的阿波利波蛋白B-100 (apo B-100) 涉及到聚合.

研究的目的:

为了研究apo B-100.00的α2域的amyloidogenic特性.
为了在α2域内识别有助于LDL聚合的特定.

主要方法:

在二次结构预测和分子动力学模拟的apo B-100 α2域螺旋.
已识别的螺旋 (k,m,p) 的合成和光谱表征.
试验室内动态聚合测试,循环二元化和传输电子显微镜以评估粉样蛋白的形成.

主要成果:

分子动力学模拟确定了k和p螺旋是最不稳定的,容易形成β片.
合成的 k 和 p 在体外形成可检测的粉样蛋白结构.
与Helix k相比,peptide p表现出明显更高的氨基原性潜力.

结论:

在apo B-100 α2域内,特定的螺旋区域具有氨基化性质.
来自这些区域的,特别是螺旋 p,可以形成粉样纤维.
这些发现表明,通过apo B-100错误折叠引发动脉硬化中的LDL聚合的机制.

关键词:

在 Ab initio 结构预测预测.阿尔法−2 域粉样纤维细胞的形成.亚脂蛋白B-100是一种阿波利波蛋白.动脉样硬化是一种动脉样硬化.在LDL聚合的LDL聚合.分子动力学模拟模型

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