Wang D, Guo L, Zhang J, Jones L R, Chen Z, Pritchard C, Roeske R W
Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis 46202-5122, USA.
J Pept Res. 2001 Apr;57(4):301-6. doi: 10.1046/j.1397-002x.2000.00823.x.
A new cyclic peptide 1 having an (LLLD)3 configuration pattern was designed that is capable of forming artificial transmembrane ion channels by self-assembly of planar peptide rings, with hydrophilic groups arrayed in the interior of the channel. Ion permeability in the presence of the synthetic peptide 1, cyclo[-Trp-Dap-Leu-D-Ala-Trp-Ser-Val-D-Ala-Trp-Ser-Ile-Gly-] (Dap: L-diaminopropionic acid), was observed in lipid bilayer membranes. The pH dependence of ionic conductance showed that the beta-amino group of Dap may play a role in the conductance of the peptide channels. Fourier-transform infrared and circular dichroism data imply that, in a membrane, a stack of cyclic peptides is formed in which the inter peptide H bonds form a kind of beta-structure analogous to that in the gramicidin A dimer and distinct from the H-bonding pattern of the beta-barrels.
设计了一种具有(LLLD)3构型模式的新型环肽1，它能够通过平面肽环的自组装形成人工跨膜离子通道，亲水基团排列在通道内部。在脂质双分子层膜中观察到合成肽1（环[ -色氨酸-二氨基丙酸-亮氨酸-D-丙氨酸-色氨酸-丝氨酸-缬氨酸-D-丙氨酸-色氨酸-丝氨酸-异亮氨酸-甘氨酸-]，二氨基丙酸为L-二氨基丙酸）存在时的离子通透性。离子电导的pH依赖性表明，二氨基丙酸的β-氨基可能在肽通道的电导中起作用。傅里叶变换红外光谱和圆二色性数据表明，在膜中形成了一堆环肽，其中肽间氢键形成了一种类似于短杆菌肽A二聚体中的β-结构，且不同于β-桶的氢键模式。
