Heller Markus, Sukopp Martin, Tsomaia Natia, John Michael, Mierke Dale F, Reif Bernd, Kessler Horst
Department Chemie, Technische Universität München, Lichtenbergstrasse 4, 85747 Garching, Germany.
J Am Chem Soc. 2006 Oct 25;128(42):13806-14. doi: 10.1021/ja063174a.
The conformation of the cyclic pentapeptide cyclo(-D-Pro-Ala(4)-) in solution and in the solid state was reinvestigated using modern NMR techniques. To allow unequivocal characterization of hydrogen bonds, relaxation behavior, and intramolecular distances, differently labeled isotopomers were synthesized. The NMR results, supported by extensive MD simulations, demonstrate unambiguously that the preferred conformation previously described by us, but recently questioned, is indeed correct. The validation of the conformational preferences of this cyclic peptide is important given that this system is a template for several bioactive compounds and for controlled "spatial screening" for the search of bioactive conformations.
利用现代核磁共振技术，对环状五肽环（-D-脯氨酸-丙氨酸（4）-）在溶液和固态中的构象进行了重新研究。为了明确表征氢键、弛豫行为和分子内距离，合成了不同标记的同位素异构体。核磁共振结果在大量分子动力学模拟的支持下，明确证明了我们之前描述但最近受到质疑的优选构象确实是正确的。鉴于该系统是几种生物活性化合物的模板以及用于寻找生物活性构象的受控“空间筛选”，验证该环肽的构象偏好非常重要。
