Department of Chemical Engineering and Materials Science, University of Minnesota, Minneapolis, MN 55455, USA.
Department of Chemical Engineering and Materials Science, University of Minnesota, Minneapolis, MN 55455, USA.
J Colloid Interface Sci. 2023 Jan;629(Pt A):125-135. doi: 10.1016/j.jcis.2022.08.051. Epub 2022 Aug 13.
The surface dilatational and shear moduli of surfactant and protein interfacial layers can be derived from surface pressures measured with a Wilhelmy plate parallel, ΔΠ and perpendicular ΔΠ to the barriers in a Langmuir trough.
Applying area oscillations, A+ ΔAe, in a rectangular Langmuir trough induces changes in surface pressure, ΔΠ and ΔΠ for monolayers of soluble palmitoyl-lysophosphatidylcholine (LysoPC), insoluble dipalmitoylphosphatidylcholine (DPPC), and the protein β-lactoglobulin to evaluate E+G=AΔΠΔA and E-G=AΔΠΔA. G was independently measured with a double-wall ring apparatus (DWR) and E by area oscillations of hemispherical bubbles in a capillary pressure microtensiometer (CPM) and the results were compared to the trough measurements.
For LysoPC and DPPC, AΔΠΔA≅AΔΠΔA meaning E≫G and E≅AΔΠΔA≅AΔΠΔA. Trough values for E were quantitatively similar to CPM when corrected for interfacial curvature. DWR showed G was 4 orders of magnitude smaller than E for both LysoPC and DPPC. For β-lactoglobulin films, AΔΠΔA>AΔΠΔA and E and G were in qualitative agreement with independent CPM and DWR measurements. For β-lactoglobulin, both E and G varied with film age and history on the trough, suggesting the evolution of the protein structure.
可以从在 Langmuir 槽中平行于(ΔΠ)和垂直于(ΔΠ)障碍物测量的表面压力中得出表面活性剂和蛋白质界面层的表面扩张和剪切弹性模量。
在矩形 Langmuir 槽中施加面积振荡,A+ΔAe,会引起表面压力、ΔΠ和可溶性棕榈酰-溶血磷脂酰胆碱(LysoPC)、不溶性二棕榈酰磷脂酰胆碱(DPPC)和蛋白质β-乳球蛋白单层的变化,以评估 E+G=AΔΠΔA 和 E-G=AΔΠΔA。使用双壁环装置(DWR)独立测量 G,并使用毛细管压力微张力计(CPM)中的半球形气泡的面积振荡测量 E,并将结果与槽测量结果进行比较。
对于 LysoPC 和 DPPC,AΔΠΔA≅AΔΠΔA 意味着 E≫G 和 E≅AΔΠΔA≅AΔΠΔA。当校正界面曲率时,槽中 E 的值与 CPM 的值在数量上相似。DWR 显示对于 LysoPC 和 DPPC,G 比 E 小 4 个数量级。对于β-乳球蛋白膜,AΔΠΔA>AΔΠΔA,并且 E 和 G 与独立的 CPM 和 DWR 测量结果在定性上一致。对于β-乳球蛋白,E 和 G 都随膜龄和槽中的历史而变化,表明蛋白质结构的演变。