Nanomechanics and intermolecular forces of amyloid revealed by four-dimensional electron microscopy

摘要: The amyloid state of polypeptides is a stable, highly organized structural form consisting laterally associated β-sheet protofilaments that may be adopted as an alternative to the functional, native state. Identifying balance forces stabilizing fundamental understanding wide accessibility this peptides and proteins with unrelated primary sequences, various chain lengths, widely differing structures. Here, we use four-dimensional electron microscopy demonstrate acting stabilize at atomic level are anisotropic, optimized interbackbone hydrogen-bonding network within β-sheets confers 20 times more rigidity on structure than sequence-specific sidechain interactions between sheets, electrostatic attraction only slightly stronger these weak amphiphilic interactions. potential biological relevance deposition such anisotropic biomaterial in vivo discussed.