Biophysical studies of membrane-peptide interactions and silk proteins

我们的研究计划的目标之一是了解生物膜的组成部分及其功能的结构，动力学和相互作用之间的关系。这些系统在我们的实验室中进行了研究，结合新的固态NMR方法。补充的结果也得到了溶液NMR，红外和荧光光谱。多重耐药细菌的出现急剧增加，导致人们做出相当大的努力来寻找对抗病原体耐药性的新方法。我们在这个建议中描述的膜相互作用的新型两亲性阳离子肽，具有天然抗菌肽的特性的研究。将研究几个方面，如肽在膜中的取向和结构以及孔形成的机制。淀粉样蛋白的异常聚集见于多种疾病。我们感兴趣的是膜的相互作用和结构的肽TTR（10-20）来自甲状腺素运载蛋白，一个127个氨基酸的淀粉样蛋白，和一个肽对应于一个保守的疏水区在人朊病毒蛋白的研究。

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.