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Hammarstroem, P; Ali, M M; Mishra, R; Tengvall, P; Lundstroem, I; Svensson, S, E-mail: ingemar@ifm.liu.se2008
AbstractAbstract
[en] A hydrophobic surface incubated in a solution of protein molecules (insulin monomers) was made into a catalytic surface for amyloid fibril formation by repeatedly incubate, rinse and dry the surface. The present contribution describes how this unexpected transformation occurred and its relation to rapid fibrillation of insulin solutions in contact with the surface. A tentative model of the properties of the catalytic surface is given, corroborated by ellipsometric measurements of the thickness of the organic layer on the surface and by atomic force microscopy. The surfaces used were spontaneously oxidized silicon made hydrophobic through treatment in dichlorodimethylsilane
Primary Subject
Source
IVC-17: 17. international vacuum congress; Stockholm (Sweden); 2-6 Jul 2007; ICSS-13: 13. international conference on surface science; Stockholm (Sweden); 2-6 Jul 2007; ICN+T 2007: International conference on nanoscience and technology; Stockholm (Sweden); 2-6 Jul 2007; Available from http://dx.doi.org/10.1088/1742-6596/100/5/052039; Country of input: International Atomic Energy Agency (IAEA)
Record Type
Journal Article
Literature Type
Conference
Journal
Journal of Physics. Conference Series (Online); ISSN 1742-6596;
; v. 100(5); [4 p.]

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