Pithadia Amit S, Bhunia Anirban, Sribalan Rajendran, Padmini Vediappen, Fierke Carol A, Ramamoorthy Ayyalusamy
Department of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.
Department of Organic Chemistry, School of Chemistry, Madurai Kamraj University, Madurai 21, India.
Chem Commun (Camb). 2016 Jan 18;52(5):942-5. doi: 10.1039/c5cc07792c.
The deposition of aggregates of human islet amyloid polypeptide (hIAPP) has been correlated with the death of β-cells in type II diabetes mellitus. The actual molecular mechanism of cell death remains largely unknown; however, it has been postulated that the process of aggregation from monomeric hIAPP is closely involved. A possible cause of cellular toxicity may be through the disruption of structural integrity of the cell membrane by IAPP. Herein, a water-soluble curcumin derivative, CurDAc, is used to investigate the mitigation of hIAPP aggregation in the absence and presence of lipid membrane.
人胰岛淀粉样多肽(hIAPP)聚集体的沉积与II型糖尿病中β细胞的死亡相关。细胞死亡的实际分子机制在很大程度上仍然未知;然而,据推测,单体hIAPP的聚集过程密切相关。细胞毒性的一个可能原因可能是IAPP破坏了细胞膜的结构完整性。在此,使用一种水溶性姜黄素衍生物CurDAc来研究在有无脂质膜存在的情况下hIAPP聚集的缓解情况。