Nisin antimicrobial activity and structural characteristics at hydrophobic surfaces coated with the PEO-PPO-PEO triblock surfactant Pluronic F108.
Nisin antimicrobial activity and structural characteristics at hydrophobic surfaces coated with the PEO-PPO-PEO triblock surfactant Pluronic F108.
复制标题
涂有 PEO-PPO-PEO 三嵌段表面活性剂 Pluronic F108 的疏水表面的乳链菌肽抗菌活性和结构特征。
DOI：
10.1016/j.jcis.2008.02.062
复制
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;McGuire,Joseph;Neff,JenniferA
The antimicrobial peptide nisin has been observed to preferentially locate at surfaces coated with the poly[ethylene oxide]–poly[propylene oxide]–poly[ethylene oxide] (PEO–PPO–PEO) surfactant Pluronic®F108, to an extent similar to its adsorption at uncoated, hydrophobic surfaces. In order to evaluate nisin function following its adsorption to surfaces presenting pendant PEO chains, the antimicrobial activity of nisin-loaded, F108-coated polystyrene microspheres and F108-coated polyurethane catheter segments was evaluated against the Gram-positive indicator strain, Pediococcus pentosaceus. The retained biological activity of these nisin-loaded layers was evaluated after incubation in the presence and absence of blood proteins, for contact periods up to one week. While an increase in serum protein concentration reduced the retained activity on both bare hydrophobic and F108-coated materials, F108-coated surfaces retained more antimicrobial activity than the uncoated surfaces. Circular dichroism spectroscopy experiments conducted with nisin in the presence of F108-coated and uncoated, silanized silica nanoparticles suggested that nisin experienced conformational rearrangement at a greater rate and to a greater extent on bare hydrophobic surfaces relative to F108-coated surfaces. These results support the notion that immobilized, pendant PEO chains confer some degree of conformational stability to nisin while also inhibiting its exchange by blood proteins.
影响因子：
2.9
作者：
MANAVALAN, P;JOHNSON, WC
通讯作者：
JOHNSON, WC