Role of Intermolecular Forces in Defining Material Properties of Protein Nanofibrils

• Published in: Science (American Association for the Advancement of Science) Vol. 318; no. 5858; pp. 1900 - 1903
• Main Authors: Knowles, Tuomas P, Fitzpatrick, Anthony W, Meehan, Sarah, Mott, Helen R, Vendruscolo, Michele, Dobson, Christopher M, Welland, Mark E
• Format: Journal Article
• Language: English
• Published: Washington, DC American Association for the Advancement of Science 21.12.2007; The American Association for the Advancement of Science
• Subjects: alpha-Crystallin B Chain - chemistry; Amyloid - chemistry; Amyloid beta-Peptides - chemistry; Amyloids; Biological and medical sciences; Biomedical materials; Bonding; Chemical Phenomena; Chemistry; Chemistry, Physical; Colloidal state and disperse state; Elastic tissue; Elasticity; Exact sciences and technology; Fundamental and applied biological sciences. Psychology; General and physical chemistry; Humans; Hydrogen Bonding; Hydrogen bonds; Hydrophobic and Hydrophilic Interactions; Insulin; Insulin - chemistry; Interactions. Associations; Intermolecular phenomena; Lactalbumin - chemistry; Lactoglobulins - chemistry; Material properties; Materials; Materials science; Microscopy, Atomic Force; Models, Molecular; Moduli of elasticity; Molecular biology; Molecular biophysics; Molecular interactions; Muramidase - chemistry; Nanocomposites; Nanomaterials; Nanostructure; Nanostructures - chemistry; Nanotechnology; Peptide Termination Factors; Peptides; Peptides - chemistry; Physical and chemical studies. Granulometry. Electrokinetic phenomena; Prealbumin - chemistry; Prions - chemistry; Protein Conformation; Protein Structure, Tertiary; Proteins; Rigidity; Saccharomyces cerevisiae Proteins - chemistry; Solar fibrils; Stiffness; Surface Tension; Surgical implants; Intermolecular interaction; Self assembly; Molecular assembly; Polypeptide; Supramolecular structure; Nanofiber; Amyloid; Biomaterial; Nanostructure; Protein; Hydrogen bond
• ISSN: 0036-8075; 1095-9203
• DOI: 10.1126/science.1150057

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