Use este identificador para citar ou linkar para este item: http://repositorio.ufla.br/jspui/handle/1/31476
Título: Polydiacetylene/triblock copolymer nanosensor for the detection of native and free bovine serum albumin
Palavras-chave: Nanosensor
Milk protein
Fluorescence
Microcalorimetry
Zeta potential
Data do documento: Jan-2017
Editor: Elsevier
Citação: REZENDE, J. de P. et al. Polydiacetylene/triblock copolymer nanosensor for the detection of native and free bovine serum albumin. Materials Science and Engineering: C, [S.l.], v. 70, part 1, p. 535-543, Jan. 2017.
Resumo: Bovine serum albumin (BSA) has been recognized as a marker of the cow's health, milk quality, an allergenic protein and as a carrier. Its detection is important in the food, pharmaceutical and medical industries. However, traditional techniques used to detect BSA are often time-consuming, expensive, and show limited sensitivity. This paper describes properties of polydiacetylene-triblock copolymer (L64) nanosensors, synthesized to easily detect BSA. Sensor efficiency was studied as a function of nanosensor composition, polydiacetylene chemical structures, BSA conformation and hydrophobic domain availability, using spectroscopic, calorimetric, light scattering, and electrokinetic analyses. Nanosensors were sensitive to detect the average BSA concentration of milk and dairy products and discriminated between native and denatured protein through naked-eye detectable blue-to-red transition. The standard Gibbs free energy (− 10.44 < ΔG° < − 49.52 kJ M), stoichiometry complex (1 < “n” < 3), and binding constant (6.7 × 102 < Ka < 4.79 × 108 M− 1) of BSA-nanosensor complex formation established a direct relationship between nanosensor response and BSA-nanosensor interaction. BSA-nanosensor interaction was entropically (without cholesterol), and enthalpically driven (with cholesterol). Eugenol-BSA complex did not induce colorimetric transition. Polydiacetylene-L64 nanosensors are potential low-cost sensors for rapid detection of BSA, discriminating between native/denatured and free/bound protein.
URI: https://www.sciencedirect.com/science/article/pii/S0928493116311821
http://repositorio.ufla.br/jspui/handle/1/31476
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