Role of Intermolecular Forces in Defining Material Properties of Protein Nanofibrils

• DOI: 10.1126/science.1150057
• Publication Date: 2007-12-21T01:19:52Z
• Authors: Tuomas P. Knowles; Anthony W. Fitzpa...; Sarah Meehan; Helen R. Mott; Michele Vendruscolo; Christopher M. Do...; Mark E. Welland
• Keywords: Rigidity (electromagnetism); Structural rigidity; Side chain

Protein molecules have the ability to form a rich variety of natural and artificial structures materials. We show that amyloid fibrils, ordered supramolecular nanostructures are self-assembled from wide range polypeptide molecules, rigidities varying over four orders magnitude, constitute class high-performance biomaterials. elucidate molecular origin fibril material properties major contribution their rigidity stems generic interbackbone hydrogen-bonding network is modulated by variable side-chain interactions.