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Design and Construction of Large Amyloid Fibers

Biological Systems Engineering Department, Virginia Tech, 301D HABB1, Blacksburg, VA 24061, USA
Author to whom correspondence should be addressed.
Academic Editor: Stephen C. Bondy
Fibers 2015, 3(2), 90-102;
Received: 3 January 2015 / Accepted: 1 April 2015 / Published: 16 April 2015
PDF [631 KB, uploaded 16 April 2015]


Mixtures of “template” and “adder” proteins self-assemble into large amyloid fibers of varying morphology and modulus. Fibers range from low modulus, rectangular cross-sectioned tapes to high modulus, circular cross-sectioned cylinders. Varying the proteins in the mixture can elicit “in-between” morphologies, such as elliptical cross-sectioned fibers and twisted tapes, both of which have moduli in-between rectangular tapes and cylindrical fibers. Experiments on mixtures of proteins of known amino acid sequence show that control of the large amyloid fiber morphology is dependent on the amount of glutamine repeats or “Q-blocks” relative to hydrophobic side chained amino acids such as alanine, isoleucine, leucine, and valine in the adder protein. Adder proteins with only hydrophobic groups form low modulus rectangular cross-sections and increasing the Q-block content allows excess hydrogen bonding on amide groups that results in twist and higher modulus. The experimental results show that large amyloid fibers of specific shape and modulus can be designed and controlled at the molecular level. View Full-Text
Keywords: amyloid; fiber; β-sheet; protein amyloid; fiber; β-sheet; protein

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Ridgley, D.M.; Rippner, C.M.W.; Barone, J.R. Design and Construction of Large Amyloid Fibers. Fibers 2015, 3, 90-102.

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