Please use this identifier to cite or link to this item: http://hdl.handle.net/1822/13887

TitleAnalysing protein competition on self-assembled mono-layers studied with quartz crystal microbalance
Author(s)Benesch, Johan
Mano, J. F.
Reis, R. L.
KeywordsCompetitive binding
Blocking
Interfacial relaxation
Sequential adsorption
Binary protein adsorption
Issue date2010
PublisherElsevier
JournalActa Biomaterialia
Abstract(s)The mechanisms by which proteins adsorb to surfaces of biomaterials have long been of interest. The present work started with the premise that small/hard and large/soft proteins will yield different sets of normalized frequency shift and dissipation signals when studied with a quartz crystal microbalance. The aim was to evaluate the usefulness of these raw data to study protein competition using protein incubations in sequence and from mixtures of albumin (BSA) and gamma-globulin (BGG) at various ratios. Increasing the concentration of BSA decreases the adsorption of subsequently incubated BGG. For BSA/ BGG mixtures the dissipation is similar for all logarithmic molar ratios BGG/BSA below 1 but soon decreases when the molar ratio of BSA/BGG (and opposite for the normalized frequency shift) is above 1, indicating preferential binding of BGG. Modelling indicated that differences in the film shear modulus and viscosity depend more on the properties of the self-assembling mono-layers (SAMs) than on the proteins. Films high in BSA tentatively differ in film shear modulus and viscosity from that of films high in BGG but only on the hydrophobic surfaces. The results were encouraging as the raw data were deemed to be able to point at protein adsorption competition.
TypeArticle
URIhttp://hdl.handle.net/1822/13887
DOI10.1016/j.actbio.2010.03.027
ISSN1742-7061
Publisher versionwww.elsevier.com/locate/actabiomat
Peer-Reviewedyes
AccessOpen access
Appears in Collections:3B’s - Artigos em revistas/Papers in scientific journals

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