Several small aromatic molecules, such as phenol red, which is used as a nontoxic drug model, have been shown to inhibit the formation of amyloid fibrils in laboratory model systems. A goal of the research on these small aromatic compounds is to find a drug that efficiently inhibits the formation of amyloid in the brain in people with incipient Alzheimer disease. Why would molecules with aromatic substituents disrupt the formation of amyloid? O Molecules with aromatic substituents interfere with stacking of aromatic residues within fibrils. O Molecules with aromatic substituents cause highly unordered fibrils to become more structured. O Molecules with aromatic substituents prevent $\beta$ sheet formation in amyloid fibrils. O Molecules with aromatic substituents prevent $\alpha$ helix formation in amyloid fibrils.
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The question asks why molecules with aromatic substituents would disrupt the formation of amyloid fibrils. The introductory text states that these molecules inhibit amyloid fibril formation. Amyloid fibrils are known to be highly ordered structures, often Show more…
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Several small aromatic molecules, such as phenol red (used as a nontoxic drug model), have been shown to inhibit the formation of amyloid in laboratory model systems. A goal of the research on these small aromatic compounds is to find a drug that would efficiently inhibit the formation of amyloid in the brain in people with incipient Alzheimer disease. (a) Suggest why molecules with aromatic substituents would disrupt the formation of amyloid. (b) Some researchers have suggested that a drug used to treat Alzheimer disease may also be effective in treating type 2 (non-insulin-dependent) diabetes mellitus. Why might a single drug be effective in treating these two different conditions?
Choose the true statements about amyloid fibrils: Proteins that form amyloid fibrils are normally soluble. Proteins that convert to an amyloid structure form soluble fibrils. Nucleation of amyloid structure may be triggered when two beta sheet regions from two partially folded proteins associate. An amyloid fibril is stabilized by hydrophobic interactions between aromatic residues. An amyloid fibril typically forms from aggregates of misfolded peptides resulting from frameshift mutations.
Adi S.
Choose the true statements about amyloid fibrils: An amyloid fibril typically forms from aggregates of misfolded peptides resulting from frameshift mutations. Proteins that convert to an amyloid fibril structure tend to have low solubility in their native form. An amyloid fibril is stabilized by hydrophobic interactions between aromatic residues. Nucleation of amyloid structure may be triggered when two ̠-sheet regions from two partially folded proteins associate. Soluble proteins that misfold and form amyloid fibrils become insoluble.
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