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| - Interaction of Ovalbumin with Phospholipids Langmuir−Blodgett Film
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| - Interaction of native ovalbumin (OVA) with 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) Langmuir−Blodgett monolayer has been studied at the air−water interface. A compressibility study shows the positiveassociation with DPPC. Adsorption kinetics shows that the protein adsorption is a one-step process and theamount of protein adsorbed depends on the concentration of protein at the water subphase. Incorporation ofprotein into the DPPC layer is surface-pressure dependent. The compressibility study indicates that the DPPC−OVA interaction is hydrophobic in nature and structural reorganization is eminent to adjust the hydrophobicmismatch between DPPC acyl chains and OVA hydrophobic moieties. At higher pressure, OVA tends tosqueeze out from the DPPC monolayer. A nanometer scale FE-SEM image confirms this observation. Globularaggregates of protein of dimension 60−80 nm were observed in DPPC−OVA supported film. Steady-statefluorescence spectroscopy suggests that the tryptophan residues of OVA are main emitting species. The blueshift of tryptophan fluorescence in supported film may be due to the tryptophan molecule of protein exposedto the hydrophobic air phase.
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