tailieunhanh - Báo cáo khoa học: Apo a-lactalbumin and lysozyme are colocalized in their subsequently formed spherical supramolecular assembly

We have reported previously that the calcium-depleted form of bovine a-lactalbumin (apoa-LA) interacts with hen egg-white lysozyme (LYS) to form spherical supramolecular structures. These supramolecular structures contain an equimolar ratio of the two proteins. We further explore here the organization of these structures. | ỊFEBS Journal Apo a-lactalbumin and lysozyme are colocalized in their subsequently formed spherical supramolecular assembly Michael Nigen Thomas Croguennec Marie-Noelle Madec and Said Bouhallab INRA Agrocampus Rennes France Keywords assembly a-lactalbumin lysozyme microscopy microsphere Correspondence S. Bouhallab INRA Agrocampus Rennes UMR 1253 Science Technologie du Lait et de l uf 65 rue de Saint Brieuc F-35042 Rennes cedex France Fax 33 2 23 48 53 50 Tel 33 2 23 48 57 42 E-mail Received 31 August 2007 revised 4 October 2007 accepted 5 October 2007 doi We have reported previously that the calcium-depleted form of bovine a-lactalbumin apo a-LA interacts with hen egg-white lysozyme LYS to form spherical supramolecular structures. These supramolecular structures contain an equimolar ratio of the two proteins. We further explore here the organization of these structures. The spherical morphology and size of the assembled LYS apo a-LA supramolecular structures were demonstrated using confocal scanning laser microscopy and scanning electron microscopy. From confocal scanning laser microscopy experiments with labelled proteins it was found that LYS and apo a-LA were perfectly colocalized and homogeneously distributed throughout the entire three-dimensional structure of the microspheres formed. The spatial colocalization of the two proteins was also confirmed by the occurrence of a fluorescence resonance energy transfer phenomenon between labelled apo a-LA and labelled LYS. Polarized light microscopy analysis revealed that the microspheres formed differ from spherulites a higher order semicrystalline structure. As the molecular mechanism initiating the formation of these microspheres is still unknown we discuss the potential involvement of a LYS apo a-LA heterodimer as a starting block for such a supramolecular assembly. Protein aggregation into various nano- to micrometre architectural assemblies including

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