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Tubulin Double Helix: Lateral and Longitudinal Curvature Changes of Tubulin Protofilament
Author(s) -
Lee Juncheol,
Song Chaeyeon,
Lee Jimin,
Miller Herbert P.,
Cho Hasaeam,
Gim Bopil,
Li Youli,
Feinstein Stuart C.,
Wilson Leslie,
Safinya Cyrus R.,
Choi Myung Chul
Publication year - 2020
Publication title -
small
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.785
H-Index - 236
eISSN - 1613-6829
pISSN - 1613-6810
DOI - 10.1002/smll.202001240
Subject(s) - tubulin , microtubule , helix (gastropod) , nanoscopic scale , biophysics , nanostructure , materials science , cytoskeleton , nanotechnology , supramolecular chemistry , crystallography , chemistry , biology , biochemistry , cell , ecology , snail , crystal structure , microbiology and biotechnology
By virtue of their native structures, tubulin dimers are protein building blocks that are naturally preprogrammed to assemble into microtubules (MTs), which are cytoskeletal polymers. Here, polycation‐directed (i.e., electrostatically tunable) assembly of tubulins is demonstrated by conformational changes to the tubulin protofilament in longitudinal and lateral directions, creating tubulin double helices and various tubular architectures. Synchrotron small‐angle X‐ray scattering and transmission electron microscopy reveal a remarkable range of nanoscale assembly structures: single‐ and double‐layered double‐helix tubulin tubules. The phase transitions from MTs to the new assemblies are dependent on the size and concentration of polycations. Two characteristic scales that determine the number of observed phases are the size of polycation compared to the size of tubulin (≈4 nm) and to MT diameter (≈25 nm). This work suggests the feasibility of using polycations that have scissor‐ and glue‐like properties to achieve “programmable breakdown” of protein nanotubes, tearing MTs into double‐stranded tubulins and building up previously undiscovered nanostructures. Importantly, a new role of tubulins is defined as 2D shape‐controllable building blocks for supramolecular architectures. These findings provide insight into the design of protein‐based functional materials, for example, as metallization templates for nanoscale electronic devices, molecular screws, and drug delivery vehicles.