Langmuir and Langmuir - Blodgett films of organophosphorus acid anhydrolase

Sarita V. Mello, Mustapha Mabrouki, Xihui Cao, Roger Leblanc, Tu Chen Cheng, Joseph J. DeFrank

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

In this paper, we describe the preparation and characterization of Langmuir and Langmuir-Blodgett (LB) monolayers of the enzyme organophosphorus acid anhydrolase (OPAA). Langmuir films of OPAA were characterized on different subphases, such as phosphate, ammonium carbonate, and bis-tris-propane buffers. Monolayers at the air-water interface were characterized by measuring the surface pressure and surface potential-area isotherms. In situ UV-vis absorption spectra were also recorded from the Langmuir monolayers. The enzyme activity at the air-water interface was tested by the addition of diisopropylfluorophosphate (DFP) to the subphase. LB films of OPAA were transferred to mica substrates to be studied by atomic force microscopy. Finally, a one-layer LB film of OPAA labeled with a fluorescent probe, fluorescein isothiocyanate (FITC), was deposited onto a quartz slide to be tested as sensor for DFP. The clear, pronounced response and the stability of the LB film as a DFP sensor show the potential of this system as a biosensor.

Original languageEnglish
Pages (from-to)968-973
Number of pages6
JournalBiomacromolecules
Volume4
Issue number4
DOIs
StatePublished - Jul 1 2003

Fingerprint

Aryldialkylphosphatase
Langmuir Blodgett films
Isoflurophate
Monolayers
Acids
Air
Tromethamine
Quartz
Water
Atomic Force Microscopy
Mica
Sensors
Enzyme activity
Surface potential
Biosensing Techniques
Enzymes
Fluorescein
Fluorescent Dyes
Propane
Biosensors

ASJC Scopus subject areas

  • Organic Chemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Polymers and Plastics
  • Materials Chemistry

Cite this

Mello, S. V., Mabrouki, M., Cao, X., Leblanc, R., Cheng, T. C., & DeFrank, J. J. (2003). Langmuir and Langmuir - Blodgett films of organophosphorus acid anhydrolase. Biomacromolecules, 4(4), 968-973. https://doi.org/10.1021/bm025775+

Langmuir and Langmuir - Blodgett films of organophosphorus acid anhydrolase. / Mello, Sarita V.; Mabrouki, Mustapha; Cao, Xihui; Leblanc, Roger; Cheng, Tu Chen; DeFrank, Joseph J.

In: Biomacromolecules, Vol. 4, No. 4, 01.07.2003, p. 968-973.

Research output: Contribution to journalArticle

Mello, SV, Mabrouki, M, Cao, X, Leblanc, R, Cheng, TC & DeFrank, JJ 2003, 'Langmuir and Langmuir - Blodgett films of organophosphorus acid anhydrolase', Biomacromolecules, vol. 4, no. 4, pp. 968-973. https://doi.org/10.1021/bm025775+
Mello, Sarita V. ; Mabrouki, Mustapha ; Cao, Xihui ; Leblanc, Roger ; Cheng, Tu Chen ; DeFrank, Joseph J. / Langmuir and Langmuir - Blodgett films of organophosphorus acid anhydrolase. In: Biomacromolecules. 2003 ; Vol. 4, No. 4. pp. 968-973.
@article{0fe8948048774c35857b747ea990c878,
title = "Langmuir and Langmuir - Blodgett films of organophosphorus acid anhydrolase",
abstract = "In this paper, we describe the preparation and characterization of Langmuir and Langmuir-Blodgett (LB) monolayers of the enzyme organophosphorus acid anhydrolase (OPAA). Langmuir films of OPAA were characterized on different subphases, such as phosphate, ammonium carbonate, and bis-tris-propane buffers. Monolayers at the air-water interface were characterized by measuring the surface pressure and surface potential-area isotherms. In situ UV-vis absorption spectra were also recorded from the Langmuir monolayers. The enzyme activity at the air-water interface was tested by the addition of diisopropylfluorophosphate (DFP) to the subphase. LB films of OPAA were transferred to mica substrates to be studied by atomic force microscopy. Finally, a one-layer LB film of OPAA labeled with a fluorescent probe, fluorescein isothiocyanate (FITC), was deposited onto a quartz slide to be tested as sensor for DFP. The clear, pronounced response and the stability of the LB film as a DFP sensor show the potential of this system as a biosensor.",
author = "Mello, {Sarita V.} and Mustapha Mabrouki and Xihui Cao and Roger Leblanc and Cheng, {Tu Chen} and DeFrank, {Joseph J.}",
year = "2003",
month = "7",
day = "1",
doi = "10.1021/bm025775+",
language = "English",
volume = "4",
pages = "968--973",
journal = "Biomacromolecules",
issn = "1525-7797",
publisher = "American Chemical Society",
number = "4",

}

TY - JOUR

T1 - Langmuir and Langmuir - Blodgett films of organophosphorus acid anhydrolase

AU - Mello, Sarita V.

AU - Mabrouki, Mustapha

AU - Cao, Xihui

AU - Leblanc, Roger

AU - Cheng, Tu Chen

AU - DeFrank, Joseph J.

PY - 2003/7/1

Y1 - 2003/7/1

N2 - In this paper, we describe the preparation and characterization of Langmuir and Langmuir-Blodgett (LB) monolayers of the enzyme organophosphorus acid anhydrolase (OPAA). Langmuir films of OPAA were characterized on different subphases, such as phosphate, ammonium carbonate, and bis-tris-propane buffers. Monolayers at the air-water interface were characterized by measuring the surface pressure and surface potential-area isotherms. In situ UV-vis absorption spectra were also recorded from the Langmuir monolayers. The enzyme activity at the air-water interface was tested by the addition of diisopropylfluorophosphate (DFP) to the subphase. LB films of OPAA were transferred to mica substrates to be studied by atomic force microscopy. Finally, a one-layer LB film of OPAA labeled with a fluorescent probe, fluorescein isothiocyanate (FITC), was deposited onto a quartz slide to be tested as sensor for DFP. The clear, pronounced response and the stability of the LB film as a DFP sensor show the potential of this system as a biosensor.

AB - In this paper, we describe the preparation and characterization of Langmuir and Langmuir-Blodgett (LB) monolayers of the enzyme organophosphorus acid anhydrolase (OPAA). Langmuir films of OPAA were characterized on different subphases, such as phosphate, ammonium carbonate, and bis-tris-propane buffers. Monolayers at the air-water interface were characterized by measuring the surface pressure and surface potential-area isotherms. In situ UV-vis absorption spectra were also recorded from the Langmuir monolayers. The enzyme activity at the air-water interface was tested by the addition of diisopropylfluorophosphate (DFP) to the subphase. LB films of OPAA were transferred to mica substrates to be studied by atomic force microscopy. Finally, a one-layer LB film of OPAA labeled with a fluorescent probe, fluorescein isothiocyanate (FITC), was deposited onto a quartz slide to be tested as sensor for DFP. The clear, pronounced response and the stability of the LB film as a DFP sensor show the potential of this system as a biosensor.

UR - http://www.scopus.com/inward/record.url?scp=0041696532&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0041696532&partnerID=8YFLogxK

U2 - 10.1021/bm025775+

DO - 10.1021/bm025775+

M3 - Article

C2 - 12857080

AN - SCOPUS:0041696532

VL - 4

SP - 968

EP - 973

JO - Biomacromolecules

JF - Biomacromolecules

SN - 1525-7797

IS - 4

ER -