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

载脂蛋白 A-I N 端和 C 端的相互作用

• 批准号: 7369310
• 负责人: DAVID ATKINSON
• 金额: $ 0.05万
• 依托单位: BOSTON UNIVERSITY MEDICAL CAMPUS
• 依托单位国家: 美国
• 财政年份: 2006
• 资助国家: 美国
• 起止时间: 2006-07-01 至 2007-06-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7369310
• 关键词: INTERACTIONS; APOLIPOPROTEIN; TERMINI

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

该子项目是利用NIH/NCRR资助的中心赠款提供的资源的许多研究子项目之一。子项目和研究者（PI）可能从另一个NIH来源获得主要资金，因此可以在其他CRISP条目中表示。所列机构为中心，不一定是研究者所在机构。我们实验室以前的工作和文献中的数据一致表明，人载脂蛋白A-I的N-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，已经合成了两种肽。一个代表apoA-I的N-末端的前44个氨基酸，分子量为4936;另一个是apoA-I的C-末端的最后46个残基，分子量为5244。几种生物物理方法正在被用来获得两种肽在溶液和脂质体中相互作用的证据。