Antimicrobial peptides (AMPs) are short cationic peptides with a high affinity for membranes and emerged as a promising therapeutic approach with potential for treating infectious diseases. Chemical stabilization of short peptides proved to be a successful approach for enhancing their bio-physical properties. Herein, we designed and synthesized a panel of conformationally constrained antimicrobial peptides with either α-helical or β-hairpin conformation using templating strategies. These synthetic short constrained peptides possess different topological distributions of hydrophobic and hydrophilic residues and displayed distinct antimicrobial activity. Notably, the conformationally constrained α-helical peptides displayed a faster internalization into the bacteria cells compared to their β-hairpin analogues. These synthetic short constrained peptides showed killing effects on a broad spectrum of microorganisms mainly through pore formation and membrane damage which provided a potentially promising skeleton for the next generation of stabilized antimicrobial peptides.

中文翻译：

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评估具有广谱抗菌活性的拓扑学上不同的受限抗菌肽†

抗菌肽（AMPs）是对膜具有高度亲和力的短阳离子肽，是一种有前途的治疗方法，具有治疗传染病的潜力。短肽的化学稳定被证明是增强其生物物理特性的成功方法。在这里，我们使用模板策略设计和合成了一组具有α-螺旋或β-发夹构象的构象受限的抗菌肽。这些合成的短约束肽具有疏水和亲水残基的不同拓扑分布，并显示出独特的抗菌活性。值得注意的是，与其β-发夹类似物相比，构象受约束的α-螺旋肽显示出更快的内在化进入细菌细胞。