去年夏季，坐落在南非Heidelberg的生产Valpre牌可口可乐的新的瓶装灌装装置投入生产。Lapp集团公司（LappGroup）下属的Lapp南非公司（Lapp Group Southern Africa）和他的合作伙伴1BC太阳能公司（IBCSolar）合作，设计并安装了形成规...去年夏季，坐落在南非Heidelberg的生产Valpre牌可口可乐的新的瓶装灌装装置投入生产。Lapp集团公司（LappGroup）下属的Lapp南非公司（Lapp Group Southern Africa）和他的合作伙伴1BC太阳能公司（IBCSolar）合作，设计并安装了形成规模的太阳能供电设备，展开更多
Understanding how small molecules interface with amyloid fibrils at the nanoscale is of importance for developing therapeutic treatments against amyloid-based diseases. Here, we show for the first time that human isle...Understanding how small molecules interface with amyloid fibrils at the nanoscale is of importance for developing therapeutic treatments against amyloid-based diseases. Here, we show for the first time that human islet amyloid polypeptides （LAPP） in the fibrillar form are polymorphic, ambidextrous, and possess multiple periodicities. Upon interfacing with the small molecule epigallocatechin gallate （EGCG）, IAPP aggregation was rendered off-pathway and assumed a form with soft and disordered clusters, while mature IAPP fibrils displayed kinks and branching but conserved the twisted fibril morphology. These nanoscale phenomena resulted from competitive interactions between EGCG and the IAPP amyloidogenic region, as well as end capping of the fibrils by the small molecule. This information is crucial in delineating IAPP toxicity implicated in type 2 diabetes and for developing new inhibitors against amyloidogenesis.展开更多
文摘去年夏季，坐落在南非Heidelberg的生产Valpre牌可口可乐的新的瓶装灌装装置投入生产。Lapp集团公司（LappGroup）下属的Lapp南非公司（Lapp Group Southern Africa）和他的合作伙伴1BC太阳能公司（IBCSolar）合作，设计并安装了形成规模的太阳能供电设备，
文摘Understanding how small molecules interface with amyloid fibrils at the nanoscale is of importance for developing therapeutic treatments against amyloid-based diseases. Here, we show for the first time that human islet amyloid polypeptides （LAPP） in the fibrillar form are polymorphic, ambidextrous, and possess multiple periodicities. Upon interfacing with the small molecule epigallocatechin gallate （EGCG）, IAPP aggregation was rendered off-pathway and assumed a form with soft and disordered clusters, while mature IAPP fibrils displayed kinks and branching but conserved the twisted fibril morphology. These nanoscale phenomena resulted from competitive interactions between EGCG and the IAPP amyloidogenic region, as well as end capping of the fibrils by the small molecule. This information is crucial in delineating IAPP toxicity implicated in type 2 diabetes and for developing new inhibitors against amyloidogenesis.
