Monolayer behavior of human serum albumin (HSA) at air-water interface

Raktim Sarmah, B. Sah, S. Kundu
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引用次数: 1

Abstract

Langmuir monolayers of human serum albumin (HSA) are formed on water surface at neutral pH (≈ 7.0) in absence and presence of Ca2+ ions in aqueous subphase. Compression-decompression surface pressure (π) - specific molecular area (A) isotherm cycle for both the conditions are recorded to compare the corresponding hysteresis behaviours. It is seen from the isotherms that in pure water compression curve of HSA monolayer tries to follow the decompression curve, whereas it is almost similar in presence of Ca2+ ions. Topographical features of the HSA monolayer at the air-water interface are obtained from Brewster angle microscopy (BAM). Protein films are also deposited in Si (001) substrates at lower and higher surface pressures, i.e., at 5 and 18 mN/m and are investigated by Atomic Force Microscopy (AFM) to explore out-of-plane structure and surface morphology. Although nearly homogeneous layer is formed by the HSA protein at the air-water interface before and after interaction with calcium ions, but slight conformation variation of protein takes place in presence of ions and accordingly the elastic behavior of monolayer changes under mechanical compression and expansion.Langmuir monolayers of human serum albumin (HSA) are formed on water surface at neutral pH (≈ 7.0) in absence and presence of Ca2+ ions in aqueous subphase. Compression-decompression surface pressure (π) - specific molecular area (A) isotherm cycle for both the conditions are recorded to compare the corresponding hysteresis behaviours. It is seen from the isotherms that in pure water compression curve of HSA monolayer tries to follow the decompression curve, whereas it is almost similar in presence of Ca2+ ions. Topographical features of the HSA monolayer at the air-water interface are obtained from Brewster angle microscopy (BAM). Protein films are also deposited in Si (001) substrates at lower and higher surface pressures, i.e., at 5 and 18 mN/m and are investigated by Atomic Force Microscopy (AFM) to explore out-of-plane structure and surface morphology. Although nearly homogeneous layer is formed by the HSA protein at the air-water interface before and after interaction with calcium ions, but slight c...
人血清白蛋白(HSA)在空气-水界面的单层行为
人血清白蛋白(HSA)的Langmuir单层膜在中性pH(≈7.0)下在水相中存在和不存在Ca2+离子时形成。记录两种条件下的压缩-减压表面压力(π) -比分子面积(A)等温循环,比较相应的滞后行为。从等温线可以看出,在纯水中,HSA单层的压缩曲线试图遵循减压曲线,而在Ca2+离子存在时,它几乎是相似的。利用Brewster角显微镜(BAM)获得了空气-水界面处HSA单层的形貌特征。在较低和较高的表面压力(即5和18 mN/m)下,蛋白质膜也沉积在Si(001)衬底上,并通过原子力显微镜(AFM)研究以探索面外结构和表面形态。虽然HSA蛋白与钙离子相互作用前后在空气-水界面形成了接近均匀的层,但在离子存在下,蛋白的构象发生了轻微的变化,因此单层在机械压缩和膨胀作用下的弹性行为发生了变化。人血清白蛋白(HSA)的Langmuir单层膜在中性pH(≈7.0)下在水相中存在和不存在Ca2+离子时形成。记录两种条件下的压缩-减压表面压力(π) -比分子面积(A)等温循环,比较相应的滞后行为。从等温线可以看出,在纯水中,HSA单层的压缩曲线试图遵循减压曲线,而在Ca2+离子存在时,它几乎是相似的。利用Brewster角显微镜(BAM)获得了空气-水界面处HSA单层的形貌特征。在较低和较高的表面压力(即5和18 mN/m)下,蛋白质膜也沉积在Si(001)衬底上,并通过原子力显微镜(AFM)研究以探索面外结构和表面形态。虽然HSA蛋白与钙离子相互作用前后在空气-水界面处形成了接近均匀的膜层,但与钙离子相互作用后,HSA蛋白在空气-水界面处形成了轻微的膜层。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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