Rat osseous plate alkaline phosphatase as Langmuir monolayer-An infrared study at the air-water interface

Luciano Caseli; Douglas C. Masui; Rosa P.M. Furriel; Francisco A. Leone; Maria E.D. Zaniquelli; Jhony Orbulescu; Roger M. Leblanc

doi:10.1016/j.jcis.2008.01.043

Rat osseous plate alkaline phosphatase as Langmuir monolayer-An infrared study at the air-water interface

Luciano Caseli, Douglas C. Masui, Rosa P.M. Furriel, Francisco A. Leone, Maria E.D. Zaniquelli, Jhony Orbulescu, Roger M. Leblanc

Chemistry

Research output: Contribution to journal › Article

24 Scopus citations

Abstract

A glycosylphosphatidylinositol (GPI)-anchored enzyme (rat osseous plate alkaline phosphatase-OAP) was studied as monolayer (pure and mixed with lipids) at the air-water interface. Surface pressure and surface potential-area isotherms showed that the enzyme forms a stable monolayer and exhibits a liquid-expanded state even at surface pressure as high as 30 mN m^-1. Isotherms for mixed dimyristoylphosphatidic acid (DMPA)-OAP monolayer showed the absence of a liquid-expanded/liquid-condensed phase transition as observed for pure DMPA monolayer. In both cases, pure or mixed monolayer, the enzyme preserves its native conformation under compression at the air-water interface as observed from in situ p-polarized light Fourier transform-infrared reflection-absorption spectroscopic (FT-IRRAS) measurements. Changes in orientation and conformation of the enzyme due to the presence or absence of DMPA, as well as due to the surface compression, are discussed.

Original language	English (US)
Pages (from-to)	476-482
Number of pages	7
Journal	Journal of Colloid And Interface Science
Volume	320
Issue number	2
DOIs	https://doi.org/10.1016/j.jcis.2008.01.043
State	Published - Apr 15 2008

Keywords

Air-water interface
Alkaline phosphatase
Infrared
Langmuir monolayers

ASJC Scopus subject areas

Colloid and Surface Chemistry
Physical and Theoretical Chemistry
Surfaces and Interfaces

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10.1016/j.jcis.2008.01.043

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Rat osseous plate alkaline phosphatase as Langmuir monolayer-An infrared study at the air-water interface. / Caseli, Luciano; Masui, Douglas C.; Furriel, Rosa P.M.; Leone, Francisco A.; Zaniquelli, Maria E.D.; Orbulescu, Jhony; Leblanc, Roger M.

In: Journal of Colloid And Interface Science, Vol. 320, No. 2, 15.04.2008, p. 476-482.

Research output: Contribution to journal › Article

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abstract = "A glycosylphosphatidylinositol (GPI)-anchored enzyme (rat osseous plate alkaline phosphatase-OAP) was studied as monolayer (pure and mixed with lipids) at the air-water interface. Surface pressure and surface potential-area isotherms showed that the enzyme forms a stable monolayer and exhibits a liquid-expanded state even at surface pressure as high as 30 mN m-1. Isotherms for mixed dimyristoylphosphatidic acid (DMPA)-OAP monolayer showed the absence of a liquid-expanded/liquid-condensed phase transition as observed for pure DMPA monolayer. In both cases, pure or mixed monolayer, the enzyme preserves its native conformation under compression at the air-water interface as observed from in situ p-polarized light Fourier transform-infrared reflection-absorption spectroscopic (FT-IRRAS) measurements. Changes in orientation and conformation of the enzyme due to the presence or absence of DMPA, as well as due to the surface compression, are discussed.",

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AU - Leone, Francisco A.

AU - Zaniquelli, Maria E.D.

AU - Orbulescu, Jhony

AU - Leblanc, Roger M.

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N2 - A glycosylphosphatidylinositol (GPI)-anchored enzyme (rat osseous plate alkaline phosphatase-OAP) was studied as monolayer (pure and mixed with lipids) at the air-water interface. Surface pressure and surface potential-area isotherms showed that the enzyme forms a stable monolayer and exhibits a liquid-expanded state even at surface pressure as high as 30 mN m-1. Isotherms for mixed dimyristoylphosphatidic acid (DMPA)-OAP monolayer showed the absence of a liquid-expanded/liquid-condensed phase transition as observed for pure DMPA monolayer. In both cases, pure or mixed monolayer, the enzyme preserves its native conformation under compression at the air-water interface as observed from in situ p-polarized light Fourier transform-infrared reflection-absorption spectroscopic (FT-IRRAS) measurements. Changes in orientation and conformation of the enzyme due to the presence or absence of DMPA, as well as due to the surface compression, are discussed.

AB - A glycosylphosphatidylinositol (GPI)-anchored enzyme (rat osseous plate alkaline phosphatase-OAP) was studied as monolayer (pure and mixed with lipids) at the air-water interface. Surface pressure and surface potential-area isotherms showed that the enzyme forms a stable monolayer and exhibits a liquid-expanded state even at surface pressure as high as 30 mN m-1. Isotherms for mixed dimyristoylphosphatidic acid (DMPA)-OAP monolayer showed the absence of a liquid-expanded/liquid-condensed phase transition as observed for pure DMPA monolayer. In both cases, pure or mixed monolayer, the enzyme preserves its native conformation under compression at the air-water interface as observed from in situ p-polarized light Fourier transform-infrared reflection-absorption spectroscopic (FT-IRRAS) measurements. Changes in orientation and conformation of the enzyme due to the presence or absence of DMPA, as well as due to the surface compression, are discussed.

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