INTERACTIONS OF APOLIPOPROTEIN A-I N- AND C-TERMINI

这个子项目是利用由NIH/NCRR资助的中心拨款提供的资源的许多研究子项目之一。子项目和调查员(PI)可能从另一个NIH来源获得了主要资金，因此可能会出现在其他CRISE条目中。列出的机构是针对中心的，而不一定是针对调查员的机构。我们实验室以前的工作和文献中的数据一直表明，人类载脂蛋白A-I的N-末端和C-末端非常接近，因此可能相互作用。为了研究这种潜在的相互作用，我们合成了两个多肽。一个代表N端的前44个氨基酸，分子量为4936；另一个代表apoA-I C末端的最后46个残基，分子量为5244。几种生物物理方法被用来获得这两种多肽在溶液和脂质环境中相互作用的证据。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Previous work in our lab and data in the literature have consistently suggested that the N- and C-termini of human apolipiprotein A-I are in close proximity and thus may interact with each other specifically. To study this potential interaction, two peptides have been synthesized. One represents the first 44 amino acids from the N-terminal, with a molecular weight of 4936; the other is the last 46 residues in the C-terminal of apoA-I, with a molecular weight of 5244. Several biophysical approaches are being utilized to obtain evidence for the interaction between the two peptides in solution and in a lipid environmen