Biophysical studies of membrane-peptide interactions and silk proteins

我们研究项目的目标之一是了解生物膜的结构、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研究的新型固态核磁共振方法的组合。溶液核磁共振、红外光谱和荧光光谱也得到了互补的结果。多重耐药细菌的出现急剧增加，促使人们努力寻找对抗病原体耐药性的新方法。我们在这个提议中描述了具有天然抗菌肽特性的新型两性阳离子肽的膜相互作用的研究。研究内容包括：膜中多肽的取向和结构、膜孔形成机制等。淀粉样蛋白的异常聚集见于多种疾病。我们对转甲状腺素衍生的肽TTR（10-20）的膜相互作用和结构的研究感兴趣，转甲状腺素是一种127个氨基酸的淀粉样蛋白，以及与人类朊病毒蛋白中保守疏水区域相对应的肽。

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.