The front cover picture shows a lariat noncanonical peptide scaffold presenting one half of a natural‐product‐derived warhead to human pancreatic α‐amylase. The folding of this peptide into an unusually stable 3₁₀ helix in solution is driven by a templating effect from the macrocyclic portion on the linear tail. This allows the peptide to place an l‐DOPA side chain in such a way that it forms a strong chelate interaction with one of the enzyme's catalytic carboxylate groups. The resulting nonapeptide inhibitor has remarkable potency, with K_i=480 pm. As the placement of catalytic carboxylates is conserved across all retaining glycosidases, if both halves of this warhead could be incorporated into such a peptide scaffold in the correct folded orientation, then the resulting inhibitor should be active across this class of enzymes. Its specificity could be tuned by varying the peptide side chains. More information can be found in the full paper by S. A. K. Jongkees et al. on page 2333 in Issue 23, 2017 (DOI: 10.1002/cbic.201700457).

中文翻译：

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封面：通过模仿植物黄酮醇战斗部的方法来调节可调节的糖苷酶抑制肽（ChemBioChem 23/2017）

封面图片显示了套索非规范肽支架，该支架将天然产物衍生的战斗部的一半呈现给人胰腺α-淀粉酶。该肽在溶液中折叠成异常稳定的3 ₁₀螺旋是由线性尾部大环部分的模板效应驱动的。这使得该肽能够以这种方式放置1 - DOPA侧链，从而使其与一种酶的催化羧酸酯基团形成强螯合相互作用。所得的九肽抑制剂具有显着的效价，K _i = 480 p m。由于催化羧酸盐的位置在所有保留的糖苷酶中都是保守的，因此，如果可以将两半战斗部以正确的折叠方向掺入此类肽支架中，那么所得的抑制剂应在此类酶中具有活性。可以通过改变肽的侧链来调节其特异性。在S.A.K.Jongkees等人的全文中可以找到更多信息。就在第23期，2017年2333页（：10.1002 / cbic.201700457 DOI）。