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首页> 外文期刊>Acta biomaterialia >Characterization of chemoselective surface attachment of the cationic peptide melimine and its effects on antimicrobial activity
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Characterization of chemoselective surface attachment of the cationic peptide melimine and its effects on antimicrobial activity

机译：阳离子肽美林碱的化学选择性表面附着的表征及其对抗菌活性的影响

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Antimicrobial peptides (AMPs) are promising alternatives to current treatments for bacterial infections. However, our understanding of the structural-functional relationship of tethered AMPs still requires further investigation to establish a general approach for obtaining consistent antimicrobial surfaces. In this study, we have systematically examined the effects of surface orientation of a broad-spectrum synthetic cationic peptide, melimine, on its antibacterial activity against Gram-positive and Gram-negative bacteria. The attachment of melimine to maleimide-functionalized glass was facilitated by addition of a single cysteine amino acid into the peptide sequence at the N-terminus (CysN) or C-terminus (CysC), or at position 13 (Cys13, approximately central). The successful attachment of the modified melimine was monitored using X-ray photoelectron spectroscopy and time-of-flight secondary ion mass spectrometry (ToF-SIMS) with principle component analysis. The ToF-SIMS analysis clearly demonstrated structural difference between the three orientations. The peptide density for the modified surfaces was found to be between 3.5-4.0 × 10 -9 mol cm -2 using a modified Bradford assay. The ability of the surfaces to resist Pseudomonas aeruginosa and Staphylococcus aureus colonization was compared using fluorescence confocal microscopy. Reductions in total P. aeruginosa and S. aureus adhesion of 70% (p 0.001) and 83% (p 0.001), respectively, after 48 h were observed for the melimine samples when compared to the blank control. We found that melimine attached via the N-terminus was the most effective in reducing total bacterial adhesion and bacterial viability with two- and four times (p 0.001) more activity than melimine attached via the C-terminus for P. aeruginosa and S. aureus, respectively. Furthermore, for Cys13, despite having the highest measured peptide density of the three surfaces, the higher concentration did not confer the greatest antibacterial effect. This highlights the importance of orientation of the peptides on the surface to efficacy. Our results suggest that the optimal orientation of the cationic residues is essential for maximum surface activity, whereby the optimal activity is obtained when the cationic portion is more available to interact with colonizing bacteria.
机译：抗菌肽（AMPs）是目前细菌感染治疗的有希望的替代品。但是，我们对栓系AMP的结构-功能关系的理解仍需要进一步研究，以建立获得一致的抗菌表面的通用方法。在这项研究中，我们系统地检查了广谱合成阳离子肽，美林碱的表面取向对其对革兰氏阳性和革兰氏阴性细菌的抗菌活性的影响。通过在N端（CysN）或C端（CysC）或位置13（Cys13，近似中心）的肽序列中添加一个半胱氨酸氨基酸，可以促进将吗啉连接到马来酰亚胺官能化的玻璃上。使用X射线光电子能谱和飞行时间二次离子质谱（ToF-SIMS）进行主成分分析，监测修饰的美林的成功附着。 ToF-SIMS分析清楚地表明了这三个方向之间的结构差异。使用改进的Bradford测定法，发现改性表面的肽密度在3.5-4.0×10 -9 mol cm -2之间。使用荧光共聚焦显微镜比较了表面抵抗铜绿假单胞菌和金黄色葡萄球菌定殖的能力。与空白对照相比，观察到48小时后，铜绿假单胞菌和金黄色葡萄球菌的总粘附力分别降低了70％（p <0.001）和83％（p <0.001）。我们发现，通过铜绿假单胞菌和铜绿假单胞菌通过N-末端附着的美莱因最有效地减少了总细菌粘附和细菌生存力，其活性比通过C末端附着的美利因高出两倍和四倍（p <0.001）。金黄色的。此外，对于Cys13，尽管在三个表面上测得的肽密度最高，但较高的浓度并没有带来最大的抗菌作用。这突出了表面上肽的取向对功效的重要性。我们的结果表明，阳离子残基的最佳取向对于最大的表面活性是必不可少的，从而当阳离子部分更易于与定植细菌相互作用时，可以获得最佳活性。

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