Surface Design for Immobilization of an Antimicrobial Peptide Mimic for Efficient Anti-Biofouling
Surface Design for Immobilization of an Antimicrobial Peptide Mimic for Efficient Anti-Biofouling
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DOI：
10.1002/chem.202000746
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发表时间：
2020-04-21
影响因子：
4.3
通讯作者：
Lau, King Hang Aaron
中科院分区：
文献类型：
--
作者：
Hasan, Abshar;Lee, Kyueui;Lau, King Hang Aaron
微生物表面附着对从水净化膜到生物医学植入物的各种设备产生负面影响。由聚（N-取代甘氨酸）类肽构成的抗菌肽模拟物（AMP）具有抗蛋白水解和抑制广谱微生物的作用，因此引起了人们极大的兴趣。我们研究了末端修饰的类肽AMP模拟物及其表面固定化如何影响抗菌活性。我们还展示了一种方便的表面改性策略，使炔-叠氮化物点击”耦合氨基官能化的表面。我们的研究结果证实，N-和C-末端类肽结构是不需要的抗菌活性。此外，我们的类肽固定密度和PEG系链的选择导致AMP之间的体积空间分离，与过去的研究相比，能够实现相对于细菌附着的最高AMP表面活性。我们的分析表明，空间灵活性的重要性，膜活性和AMP分离可能是一个控制参数，优化表面抗生物污损。
Microbial surface attachment negatively impacts a wide range of devices from water purification membranes to biomedical implants. Mimics of antimicrobial peptides (AMPs) constituted from poly(N-substituted glycine) peptoids" are of great interest as they resist proteolysis and can inhibit a wide spectrum of microbes. We investigate how terminal modification of a peptoid AMP-mimic and its surface immobilization affect antimicrobial activity. We also demonstrate a convenient surface modification strategy for enabling alkyne-azide click" coupling on amino-functionalized surfaces. Our results verified that the N- and C-terminal peptoid structures are not required for antimicrobial activity. Moreover, our peptoid immobilization density and choice of PEG tether resulted in a volumetric" spatial separation between AMPs that, compared to past studies, enabled the highest AMP surface activity relative to bacterial attachment. Our analysis suggests the importance of spatial flexibility for membrane activity and that AMP separation may be a controlling parameter for optimizing surface anti-biofouling.