Publication Date:
2007-12-22
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Knowles, Tuomas P -- Fitzpatrick, Anthony W -- Meehan, Sarah -- Mott, Helen R -- Vendruscolo, Michele -- Dobson, Christopher M -- Welland, Mark E -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2007 Dec 21;318(5858):1900-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Nanoscience Centre, University of Cambridge, J. J. Thomson Avenue, Cambridge CB3 0FF, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18096801" target="_blank"〉PubMed〈/a〉
Keywords:
Amyloid/*chemistry
;
Amyloid beta-Peptides/chemistry
;
Chemistry, Physical
;
Elasticity
;
Humans
;
Hydrogen Bonding
;
Hydrophobic and Hydrophilic Interactions
;
Insulin/chemistry
;
Lactalbumin/chemistry
;
Lactoglobulins/chemistry
;
Microscopy, Atomic Force
;
Models, Molecular
;
Muramidase/chemistry
;
Nanostructures/*chemistry
;
Peptide Termination Factors
;
Peptides/*chemistry
;
Physicochemical Phenomena
;
Prealbumin/chemistry
;
Prions/chemistry
;
Protein Conformation
;
Protein Structure, Tertiary
;
Saccharomyces cerevisiae Proteins/chemistry
;
Surface Tension
;
alpha-Crystallin B Chain/chemistry
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
Permalink
