BACKGROUND: One of the challenges of current researches in biotechnological field is the achievement of regular and increasingly smaller protein crystals for genomics and biocatalyst applications. The membrane contactor-based methodology appears a time-effectiveness and economically competitive technology for accomplishing this target. RESULTS: Here, a new class of interactive polymeric interfaces enabling to nucleate massively smaller protein crystals in even shorter time through controlling attractive interactions is discussed. Specifically, the role of attractive interfacial forces between a model Lysozyme solution and modified poly(vinylidene fluoride) membranes has been examined. The insertion of amphiphilic motifs in fluorinated membranes allowed quicker agglomeration of protein crystals at the membrane surface reducing significantly the induction time to the protein nucleation. The chemical nature of the modifier permitted to modulate the membrane affinity to the Lysozyme, involving polar and non polar attractive interactions and preserving intrinsic structural features, transport properties and hydrophobic character of the interfaces, according to the basics of the membrane crystallization technology. The formation of critical nuclei was observed after 3 hours and micro-sized crystals were formed in less than 24 hours. CONCLUSION: The experimental evidences suggest these membranes as a promising class of interactive interfaces that may rapidly bring to advances in genomics research.

Interactive functional poly(vinylidene fluoride) membranes with modulated Lysozyme affinity: a promising class of new interfaces for contactor crystallizers

Gugliuzza A;Drioli;
2009

Abstract

BACKGROUND: One of the challenges of current researches in biotechnological field is the achievement of regular and increasingly smaller protein crystals for genomics and biocatalyst applications. The membrane contactor-based methodology appears a time-effectiveness and economically competitive technology for accomplishing this target. RESULTS: Here, a new class of interactive polymeric interfaces enabling to nucleate massively smaller protein crystals in even shorter time through controlling attractive interactions is discussed. Specifically, the role of attractive interfacial forces between a model Lysozyme solution and modified poly(vinylidene fluoride) membranes has been examined. The insertion of amphiphilic motifs in fluorinated membranes allowed quicker agglomeration of protein crystals at the membrane surface reducing significantly the induction time to the protein nucleation. The chemical nature of the modifier permitted to modulate the membrane affinity to the Lysozyme, involving polar and non polar attractive interactions and preserving intrinsic structural features, transport properties and hydrophobic character of the interfaces, according to the basics of the membrane crystallization technology. The formation of critical nuclei was observed after 3 hours and micro-sized crystals were formed in less than 24 hours. CONCLUSION: The experimental evidences suggest these membranes as a promising class of interactive interfaces that may rapidly bring to advances in genomics research.
2009
Istituto per la Tecnologia delle Membrane - ITM
Interfacial interactions
Membrane
Surface
Protein
Crystals
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/28906
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