Wang Deyun, Chen Kang, Dimartino Gianluca, Arora Paramjit S
Department of Chemistry, New York University, New York, NY 10003, USA.
Org Biomol Chem. 2006 Nov 21;4(22):4074-81. doi: 10.1039/b612891b.
We have reported a new class of artificial alpha-helices in which a pre-organized alpha-turn nucleates the helical conformation [R. N. Chapman, G. Dimartino, and P. S. Arora, J Am. Chem. Soc., 2004, 126, 12252 and D. Wang, K. Chen, J. L. Kulp, III, and P. S. Arora, J. Am. Chem. Soc., 2006, 128, 9248]. This manuscript describes the effect of the core nucleation template on the overall helicity of the peptides and demonstrates that the macrocycle which most closely mimics the 13-membered hydrogen-bonded alpha-turn in canonical alpha-helices also affords the most stable artificial alpha-helix. We also investigate the stability of these synthetic helices through classical helix-coil parameters and find that the denaturation behavior of HBS alpha-helices agrees with the theoretical properties of a peptide with a well-defined and stable helix nucleus.
我们报道了一类新型人工α-螺旋,其中预先构建的α-转角促使螺旋构象成核[R. N. 查普曼、G. 迪马蒂诺和P. S. 阿罗拉,《美国化学会志》,2004年,126卷,12252页;以及D. 王、K. 陈、J. L. 库尔普三世和P. S. 阿罗拉,《美国化学会志》,2006年,128卷,9248页]。本手稿描述了核心成核模板对肽整体螺旋度的影响,并证明在典型α-螺旋中最紧密模拟13元氢键α-转角的大环也能提供最稳定的人工α-螺旋。我们还通过经典的螺旋-卷曲参数研究了这些合成螺旋的稳定性,发现HBSα-螺旋的变性行为与具有明确且稳定螺旋核的肽的理论性质相符。