Frankiewicz Lukasz, Betti Cecilia, Guillemyn Karel, Tourwé Dirk, Jacquot Yves, Ballet Steven
Department of Organic Chemistry, Vrije Universiteit Brussel, Pleinlaan 2, B-1050, Brussels, Belgium.
J Pept Sci. 2013 Jul;19(7):423-32. doi: 10.1002/psc.2515. Epub 2013 May 27.
A model octapeptide segment derived from vasoactive intestinal peptide (VIP) was utilised to investigate the effect of several conventional cyclisation methods on the α-helical conformation in short peptide fragments. Three of the classical macrocyclisation techniques (i.e. lactamisation, ring-closing metathesis and Huisgen cycloaddition) were applied, and the conformations of the resulting cyclic peptides, as well as their linear precursors, were compared by CD analysis. The visibly higher folding propensity of the triazole-tethered peptide after azide-alkyne CuAAC macrocyclisation illustrates that the secondary structure of a short peptide fragment can differ significantly depending on the chemical strategy used to covalently cross-link side chain residues in a 'helical' fragment.
利用一段源自血管活性肠肽（VIP）的模型八肽片段，研究了几种传统环化方法对短肽片段中α-螺旋构象的影响。应用了三种经典的大环化技术（即内酰胺化、闭环复分解反应和惠斯根环加成反应），并通过圆二色光谱（CD）分析比较了所得环肽及其线性前体的构象。叠氮化物-炔烃铜催化的点击化学（CuAAC）大环化反应后，三唑连接的肽具有明显更高的折叠倾向，这表明短肽片段的二级结构可能会因用于在“螺旋”片段中对侧链残基进行共价交联的化学策略而有显著差异。
