A Designed Protein Interface That Blocks Fibril Formation
نویسندگان
چکیده
منابع مشابه
A designed protein interface that blocks fibril formation.
Protein fibril formation is implicated in many diseases, and therefore much effort has been focused toward the development of inhibitors of this process. In a previous project, a monomeric protein was computationally engineered to bind itself and form a heterodimer complex following interfacial redesign. One of the protein monomers, termed monomer-B, was unintentionally destabilized and shown t...
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The origins of formation of an intermediate state involved in amyloid formation and ways to prevent it are illustrated with the example of the Formin binding protein 28 (FBP28) WW domain, which folds with biphasic kinetics. Molecular dynamics of protein folding trajectories are used to examine local and global motions and the time dependence of formation of contacts between C(α)s and C(β)s of s...
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Insoluble protein fibrils resulting from the self-assembly of a conformational intermediate are implicated as the causative agent in several severe human amyloid diseases, including Alzheimer's disease, familial amyloid polyneuropathy, and senile systemic amyloidosis. The latter two diseases are associated with transthyretin (TTR) amyloid fibrils, which appear to form in the acidic partial dena...
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Soluble rat tail tendon collagen with intact nonhelical ends and largely free of aggregates was used to study fibril formation in vitro. The process was initiated by raising the pH and warming a cold solution of collagen. Fibril formation was monitored by turbidity and the product was examined by electron microscopy. Optimal conditions that will form fibrils similar to those observed in vivo ar...
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Collagen is most abundant in animal tissues as very long fibrils with a characteristic axial periodic structure. The fibrils provide the major biomechanical scaffold for cell attachment and anchorage of macromolecules, allowing the shape and form of tissues to be defined and maintained. How the fibrils are formed from their monomeric precursors is the primary concern of this review. Collagen fi...
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ژورنال
عنوان ژورنال: Journal of the American Chemical Society
سال: 2004
ISSN: 0002-7863,1520-5126
DOI: 10.1021/ja0456858