Toniolo Claudio, Crisma Marco, Formaggio Fernando, Peggion Cristina, Broxterman Quirinus B, Kaptein Bernard
Institute of Biomolecular Chemistry, CNR, Department of Organic Chemistry, University of Padova, 35131 Padova, Italy.
Biopolymers. 2004;76(2):162-76. doi: 10.1002/bip.10575.
A proper understanding of the detailed nature and mechanism of physicochemical interactions depends heavily upon our ability to design and synthesize conformationally constrained 3D structures whose intercomponent geometry (either rigorously rigid or able to undergo destructuration, if required, but in all cases precisely tunable) would be well defined. To this end we have recently reported a few initial studies and we are currently working on the exploitation of stable, short, helical peptide spacers based on achiral and/or chiral Calpha-tetrasubstituted alpha-amino acids. These building blocks are known to force the peptides either to predominantly fold into a 3(10)-helical structure or to adopt a fully extended, planar 2.0(5)-helix. The systems under investigation involve a donor and an acceptor moiety linked to the N- and C-termini of the oligopeptide spacer main chain. By increasing the number of intervening residues the donor.acceptor separation can be easily modulated. This review highlights details of these two novel peptide secondary structures and their use as molecular spacers in physicochemical investigations.
对物理化学相互作用的详细性质和机制的正确理解在很大程度上取决于我们设计和合成构象受限的三维结构的能力，其组件间几何结构（要么严格刚性，要么在需要时能够解构，但在所有情况下都能精确调节）将得到很好的定义。为此，我们最近报告了一些初步研究，目前正在研究基于非手性和/或手性α-碳四取代α-氨基酸的稳定、短螺旋肽间隔物。已知这些构建块会迫使肽主要折叠成3(10)-螺旋结构或采用完全伸展的平面2.0(5)-螺旋结构。所研究的系统涉及与寡肽间隔物主链的N端和C端相连的供体和受体部分。通过增加中间残基的数量，可以轻松调节供体-受体间距。本综述重点介绍了这两种新型肽二级结构的细节及其在物理化学研究中作为分子间隔物的用途。
