Nisin adsorption to hydrophobic surfaces coated with the PEO-PPO-PEO triblock surfactant Pluronic F108.
Nisin adsorption to hydrophobic surfaces coated with the PEO-PPO-PEO triblock surfactant Pluronic F108.
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乳链菌肽吸附于涂有 PEO-PPO-PEO 三嵌段表面活性剂 Pluronic F108 的疏水表面。
DOI：
10.1016/j.jcis.2008.02.053
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发表时间：
2008
影响因子：
9.9
通讯作者：
Neff,JenniferA
中科院分区：
文献类型：
--
作者：
Tai,Yuan-Ching;Joshi,Pranav;McGuire,Joseph;Neff,JenniferA
The adsorption and elution of the antimicrobial peptide nisin at hydrophobic, silanized silica surfaces coated with the poly(ethylene oxide)–poly(propylene oxide)–poly(ethylene oxide) surfactant Pluronic®F108 were measured in situ, with ellipsometry. While such layers are known to inhibit protein adsorption, nisin was observed to adsorb in multilayer quantities, to an extent similar to its adsorption at uncoated, hydrophobic surfaces. The rates of nisin adsorption and elution were generally slower at F108-coated surfaces. And, the sequential adsorption of nisin, including two adsorption–elution cycles at each surface, showed greater differences in adsorption rates between the first and second adsorption cycles, when evaluated at identical mass density, for uncoated relative to F108-coated surfaces. These results indicate that nisin adsorption occurs via “entrapment” within the PEO brush layer at F108-coated surfaces, in this way slowing adsorption and spontaneous elution, and inhibiting post-adsorptive molecular rearrangements by reducing the lateral mobility of nisin. While F108-coated layers rejected adsorption of serum albumin, sequential adsorption experiments carried out with nisin and albumin showed a low level of albumin adsorption when nisin was present at the interface.
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