SFPE5 STRUCTURE: 19F-1H NOE

SFPE5 结构：19F-1H NOE

• 批准号: 7598701
• 负责人: Helen E. Blackwell
• 金额: $ 0.85万
• 依托单位: UNIVERSITY OF WISCONSIN-MADISON
• 依托单位国家: 美国
• 财政年份: 2007
• 资助国家: 美国
• 起止时间: 2007-03-01 至 2008-02-29
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7598701
• 关键词: Adopted; Amides; Amines; Biomimetics; Class; Compatible; Computer Retrieval of Information on Scientific Projects Database; Development; Electrostatics; Funding; Glycine; Grant; Helix (Snails); Institution; Length; Molecular Conformation; N-substituted Glycines; Peptides; Peptoids; Polymers; Relative (related person); Research; Research Personnel; Resources; Role; Side; Source; Structure; United States National Institutes of Health; Work; analog; design; ear helix; ethylamine; monomer; novel; nuclear Overhauser enhancement; polyproline

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. Oligomers of N-substituted glycines, or peptoids, are an important class of non-native polymers whose close structural similarity to natural a-peptides and ease of synthesis offer significant advantages for the study of biomolecular interactions and the development of biomimetics. Peptoids that are N-substituted with a-chiral aromatic amide side chains have been shown to adopt stable helical conformations reminiscent of the polyproline type-I helix. Elucidation of the factors involved in peptoid helix formation is essential for the development of general rules for the design of peptoids with discreet and novel structures. Here, we investigate the effects of pentafluorophenyl functionality on the conformational profiles of the peptoid helix. This work is enabled by the synthesis of a new a-chiral amine building block, (S)-1-(pentafluorophenyl)ethylamine (S-2), that was found to be highly compatible with peptoid synthesis (delivering (S)-N-(1-(pentafluorophenyl)ethyl)glycine oligomers). The strategic incorporation of this perfluorinated monomer unit is allowing us to probe both the potential for ?-stacking interactions along the side of peptoid helices and the role of side chain electrostatics in peptoid folding. Initial studies revealed that (S)-N-(1-(pentafluorophenyl)ethyl)glycine monomers stabilize helical peptoid structures at significantly shorter lengths relative to non-fluorinated peptoid analogues.

该子项目是利用该技术的众多研究子项目之一 资源由 NIH/NCRR 资助的中心拨款提供。子项目和 研究者 (PI) 可能已从 NIH 的另一个来源获得主要资金， 因此可以在其他 CRISP 条目中表示。列出的机构是 对于中心来说，它不一定是研究者的机构。 N-取代甘氨酸寡聚物或类肽是一类重要的非天然聚合物，其结构与天然α肽非常相似且易于合成，为生物分子相互作用的研究和仿生学的开发提供了显着的优势。用非手性芳香酰胺侧链进行 N 取代的类肽已被证明采用稳定的螺旋构象，让人想起聚脯氨酸 I 型螺旋。阐明类肽螺旋形成中涉及的因素对于制定具有谨慎和新颖结构的类肽设计的一般规则至关重要。在这里，我们研究了五氟苯基功能性对类肽螺旋构象特征的影响。这项工作是通过合成一种新的α-手性胺结构单元（S）-1-（五氟苯基）乙胺（S-2）来实现的，人们发现它与类肽合成（提供（S）-N-（1-（五氟苯基）乙基）甘氨酸低聚物）高度兼容。这种全氟化单体单元的策略性合并使我们能够探索类肽螺旋侧面的β-堆积相互作用的潜力以及侧链静电在类肽折叠中的作用。初步研究表明，与非氟化类肽类似物相比，(S)-N-(1-(五氟苯基)乙基)甘氨酸单体以显着更短的长度稳定螺旋类肽结构。