Using lattice models we explore the factors that determine the tendencies of polypeptide chains to aggregate by exhaustively sampling the sequence and conformational space. The morphologies of the fibril-like structures and the time scales (τ(fib)) for their formation depend on a balance between hydrophobic and Coulomb interactions. The extent of population of an ensemble of N* structures, whic...

BACKGROUND The capacity of a polypeptide chain to engage in an amyloid formation process and cause a conformational disease is contained in its sequence. Some of the sequences undergoing fibrillation contain critical methionine (Met) residues which in vivo can be synthetically substituted by selenomethionine (SeM) and alter their properties. METHODOLOGY/PRINCIPAL FINDINGS Using peptide synthe...

Fibronectin binding sites on cultured human fibroblasts were localized by high voltage electron microscopy using either 5- or 18-nm colloidal gold beads (Au5 or Au18) bound to intact fibronectin, the 70-kD amino-terminal fragment of fibronectin that blocks incorporation of exogenous fibronectin into extracellular matrix, or 160-180-kD fragments of fibronectin with cell adhesion and heparin-bind...

Quasielastic light scattering (QLS) spectroscopy is a noninvasive optical method for studying the dynamic properties of macromolecular solutions. Its most important application is the determination of diffusion coefficients, from which the sizes of particles in solution may be estimated. The technique thus is particularly useful for monitoring assembly (polymerization and aggregation) reactions...

Protein aggregation with the concomitant formation of amyloid fibrils is related to several neurodegenerative diseases, but also to non-neuropathic amyloidogenic diseases and non-neurophatic systemic amyloidosis. Lysozyme is the protein involved in the latter, and it is widely used as a model system to study the mechanisms underlying fibril formation and its inhibition. Several phenolic compoun...

T amyloidoses are diseases of protein conformation, in which a particular soluble innocuous protein transforms and aggregates into an insoluble fibrillar structure that deposits in extracellular spaces of specific organs (reviewed in refs. 1–4). Organ dysfunction accompanies fibrillar deposition, and the amyloid hypothesis proposes a cause and effect relationship between deposition and dysfunct...