在水中具有非凡稳定性的单圈肽α螺旋。
Single turn peptide alpha helices with exceptional stability in water.
作者信息
Shepherd Nicholas E, Hoang Huy N, Abbenante Giovanni, Fairlie David P
机构信息
Centre for Drug Design and Development, Institute for Molecular Bioscience, University of Queensland, Brisbane, Qld 4072, Australia.
出版信息
J Am Chem Soc. 2005 Mar 9;127(9):2974-83. doi: 10.1021/ja0456003.
Cyclic pentapeptides are not known to exist in alpha-helical conformations. CD and NMR spectra show that specific 20-membered cyclic pentapeptides, Ac-(cyclo-1,5) [KxxxD]-NH(2) and Ac-(cyclo-2,6)-R[KxxxD]-NH(2), are highly alpha-helical structures in water and independent of concentration, TFE, denaturants, and proteases. These are the smallest alpha-helical peptides in water.
已知环状五肽不存在α-螺旋构象。圆二色光谱（CD）和核磁共振光谱（NMR）表明，特定的20元环状五肽，即Ac-(环-1,5)[KxxxD]-NH₂和Ac-(环-2,6)-R[KxxxD]-NH₂，在水中呈高度α-螺旋结构，且与浓度、三氟乙醇（TFE）、变性剂和蛋白酶无关。这些是水中最小的α-螺旋肽。
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