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Author
R. Ni
J.M. Kleijn
S. Abeln
M.A. Cohen Stuart
P.G. Bolhuis
Year
2015
Title
Competition between surface adsorption and folding of fibril-forming polypeptides
Journal
Physical Review E
Volume | Issue number
91 | 2
Pages (from-to)
022711
Number of pages
5
Document type
Article
Faculty
Faculty of Science (FNWI)
Institute
Van 't Hoff Institute for Molecular Sciences (HIMS)
Abstract
Self-assembly of polypeptides into fibrillar structures can be initiated by planar surfaces that interact favorably with certain residues. Using a coarse-grained model, we systematically studied the folding and adsorption behavior of a beta-roll forming polypeptide. We find that there are two different folding pathways depending on the temperature: (i) at low temperature, the polypeptide folds in solution into a beta-roll before adsorbing onto the attractive surface; (ii) at higher temperature, the polypeptide first adsorbs in a disordered state and folds while on the surface. The folding temperature increases with increasing attraction as the folded beta-roll is stabilized by the surface. Surprisingly, further increasing the attraction lowers the folding temperature again, as strong attraction also stabilizes the adsorbed disordered state, which competes with folding of the polypeptide. Our results suggest that to enhance the folding, one should use a weakly attractive surface. They also explain the recent experimental observation of the nonmonotonic effect of charge on the fibril formation on an oppositely charged surface [C. Charbonneau et al., ACS Nano 8, 2328 ( 2014)].
URL
go to publisher's site
Language
English
Permalink
http://hdl.handle.net/11245/1.473523
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  • Competition between surface adsorption

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