Adsorption mechanism of myelin basic protein on model substrates and its bridging interaction between the two surfaces

Myelin basic protein (MBP) is an intrinsically disordered (unstructured) protein known to play an important role in the stability of myelin's multilamellar membrane structure in the central nervous system. The adsorption of MBP and its capacity to interact with and bridge solid substrates has b...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1985. - 31(2015), 10 vom: 17. März, Seite 3159-66
1. Verfasser: Lee, Dong Woog (VerfasserIn)
Weitere Verfasser: Banquy, Xavier, Kristiansen, Kai, Min, Younjin, Ramachandran, Arun, Boggs, Joan M, Israelachvili, Jacob N
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2015
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Aluminum Silicates Lipid Bilayers Myelin Basic Protein mica V8A1AW0880
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520 |a Myelin basic protein (MBP) is an intrinsically disordered (unstructured) protein known to play an important role in the stability of myelin's multilamellar membrane structure in the central nervous system. The adsorption of MBP and its capacity to interact with and bridge solid substrates has been studied using a surface forces apparatus (SFA) and a quartz crystal microbalance with dissipation (QCM-D). Adsorption experiments show that MBP molecules adsorb to the surfaces in a swollen state before undergoing a conformational change into a more compact structure with a thickness of ∼3 nm. Moreover, this compact structure is able to interact with nearby mica surfaces to form adhesive bridges. The measured adhesion force (energy) between two bridged surfaces is 1.0 ± 0.1 mN/m, (Ead = 0.21 ± 0.02 mJ/m(2)), which is slightly smaller than our previously reported adhesion force of 1.7 mN/m (Ead = 0.36 mJ/m(2)) for MBP adsorbed on two supported lipid bilayers (Lee et al., Proc. Natl. Acad. Sci. U.S.A. 2014, 111, E768-E775). The saturated surface concentration of compact MBP on a single SiO2 surface reaches a stable value of 310 ± 10 ng/cm(2) regardless of the bulk MBP concentration. A kinetic three-step adsorption model was developed that accurately fits the adsorption data. The developed model is a general model, not limited to intrinsically disordered proteins, that can be extended to the adsorption of various chemical compounds that undergo chemical reactions and/or conformational changes upon adsorbing to surfaces. Taken together with our previously published data (Lee et al., Proc. Natl. Acad. Sci. U.S.A. 2014, 111, E768-E775), the present results confirm that conformational changes of MBP upon adsorption are a key for strong adhesion, and that such conformational changes are strongly dependent on the nature of the surfaces 
650 4 |a Journal Article 
650 4 |a Research Support, N.I.H., Extramural 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a Research Support, U.S. Gov't, Non-P.H.S. 
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650 7 |a Lipid Bilayers  |2 NLM 
650 7 |a Myelin Basic Protein  |2 NLM 
650 7 |a mica  |2 NLM 
650 7 |a V8A1AW0880  |2 NLM 
700 1 |a Banquy, Xavier  |e verfasserin  |4 aut 
700 1 |a Kristiansen, Kai  |e verfasserin  |4 aut 
700 1 |a Min, Younjin  |e verfasserin  |4 aut 
700 1 |a Ramachandran, Arun  |e verfasserin  |4 aut 
700 1 |a Boggs, Joan M  |e verfasserin  |4 aut 
700 1 |a Israelachvili, Jacob N  |e verfasserin  |4 aut 
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