Enhanced Architecture of Lipid-Carbon Nanotubes as Langmuir–Blodgett Films to Investigate the Enzyme Activity of Phospholipases from Snake Venom

The immobilization of biomolecules in films with a controlled architecture permits the access of information on the molecular interactions, not only between film components, but also between the film and substances in the external environment. In this study, we investigated the immobilization of the...

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Bibliographic Details
Published in:The journal of physical chemistry. B 2012-11, Vol.116 (45), p.13424-13429
Main Authors: Caseli, Luciano, Tiburcio, Vera L. B, Vargas, Frey F. R, Marangoni, Sérgio, Siqueira, José R
Format: Article
Language:English
Subjects:
Architecture
Biocatalysis
Catalysis
Catalysts
Enzymes
Immobilization
Langmuir-Blodgett films
Lipids - chemistry
Nanotubes, Carbon
Phospholipase
Phospholipases A2 - metabolism
Snake Venoms - enzymology
Snakes
Substrate Specificity
Surface Properties
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Summary:The immobilization of biomolecules in films with a controlled architecture permits the access of information on the molecular interactions, not only between film components, but also between the film and substances in the external environment. In this study, we investigated the immobilization of the phospholipase A2 from snake venoms (4-nitro-3-(octanoyloxy)benzoic acid, OBZ) in solid supports as a Langmuir–Blodgett (LB) film, followed by incorporation of carbon nanotubes (CNTs). The hybrid film was characterized by infrared spectroscopy and the interactions with its catalytic substrate were investigated. The presence of CNTs leads to a structure with an adequate environment to preserve the enzyme properties, leading to an optimum catalytic activity. This enhanced architecture was exploited in terms of vibrational spectroscopy, which indicated changes in the secondary structure of the enzyme upon contact with the catalytic substrate.
ISSN:1520-6106
1520-5207
DOI:10.1021/jp307585k