Biophysical studies of membrane-peptide interactions and silk proteins

我们研究计划的目标之一是了解生物膜组分的结构、动力学和相互作用与其功能之间的关系。这些系统是在我们的实验室中通过结合新的固态核磁共振方法进行研究的。溶液核磁共振、红外光谱和荧光光谱也得到了补充结果。多重耐药细菌的出现急剧增加，促使人们努力寻找新的方法来对抗病原体耐药性。在这个方案中，我们描述了具有天然抗菌肽性质的新型两亲性阳离子多肽的膜相互作用的研究。将从几个方面进行研究，如膜中多肽的取向和结构以及成孔机理。淀粉样蛋白的异常聚集存在于多种疾病中。我们感兴趣的是从转甲状腺蛋白(一种127个氨基酸的淀粉样蛋白)中提取的多肽TTR(10-20)的膜相互作用和结构的研究，以及与人蛋白中保守的疏水区相对应的多肽的结构。

One of the objectives of our research program is to understand the relationship between the structure, dynamics and interactions of the components of the biological membranes and their function. These systems are investigated in our laboratory by a combination of novel solid-state NMR approaches. Complementary results are also obtained by solution NMR, infrared and fluorescence spectroscopy. The dramatic increase in the appearance of multi-drug resistant bacteria has led to considerable efforts to find new ways to fight pathogen resistance. We describe in this proposal the study of the membrane interactions of novel amphipathic cationic peptides that possess the properties of natural antimicrobial peptides. Several aspects will be investigated, such as the orientation and structure of the peptides in membranes and the mechanism of pore formation. The abnormal aggregation of amyloid proteins is found in a variety of diseases. We are interested in the study of the membrane interactions and structure of the peptide TTR (10-20) derived from transthyretin, a 127 amino acid amyloid protein, and of a peptide corresponding to a conserved hydrophobic region in the human prion protein.