AFM force measurements on microtubule‐associated proteins: the projection domain exerts a long‐range repulsive force

FEBS Letters

Mukhopadhyay, Rajendrani¹  Hoh, Jan H.¹ 

[1] Department of Physiology, Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Baltimore, MD 21205, USA

关键词: Unstructured;    Entropic exclusion;    Microtubule-associated protein 2;    Tau;    AFM;    atomic force microscopy;    APTES;    3-aminopropyl-triethoxy-silane;    BSA;    bovine serum albumin;    IgG;    immunoglobulin G;    MAP;    microtubule-associated protein;    PIPES;    1;    4-piperazine-diethane-sulfonic acid;   

DOI  :  10.1016/S0014-5793(01)02844-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Microtubule-associated proteins (MAPs) are thought to control spacing between microtubules. We propose that the projection domain is largely unstructured and exerts a long-range repulsive force that is predominantly entropic in origin, providing a physical mechanism for maintaining spacing. To test this hypothesis, we developed an experimental system where MAPs are electrostatically end-attached to a flat surface, such that the projection domains extend away from the surface. Atomic force microscopy force measurements on this system show that projection domains exert a long-range (>100 nm) repulsive force. This force depends on the ionic strength of the solution in a way that is consistent with a polyelectrolyte polymer brush.

【 授权许可】

Unknown