Brain diseases and metalloproteins by David R. Brown

By David R. Brown

This publication describes the most recent learn on neurodegenerative ailment and metal-binding proteins. It lays powerful emphasis on biochemistry and mobilephone biology. The ailments coated within the publication contain Parkinson's disorder, Alzheimer's ailment, prion sickness, and ALS. The chapters individually research such concerns as mechanisms of steel binding, metal-induced structural adjustments in proteins, adjustments in mobile steel metabolism in illness, and makes an attempt at a healing process in response to protein steel binding.

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1994) had noted that H2O2 levels in cells treated with Aβ also reached a maximum before declining. 6 Other Aggregating Protein Systems Confirmation of the generation of H2O2 by the Aβ (1–40) and Aβ (1–42) peptides led us to query whether this property was unique to these peptides, or whether various other peptides and proteins implicated in neurodegenerative diseases (and possibly in some peripheral amyloidoss) might share this same feature. 1. , 2003) all had the ability to generate H2O2. , 2007).

Since H2O2 is generated in the immediate vicinity of the Aβ peptide, it could also be responsible for much of the oxidation of the peptide itself. Possible reactions are (i) the loss of an electron from the peptide/Cu(I) complex to form the Aβ radical cation, which then undergoes rapid rearrangement to give side chain oxidation products, (ii) a bimolecular reaction with H2O2 leading directly to peptide oxidation, (iii) the liberation of the •OH radical from H2O2 via the Fenton reaction and subsequent direct attack of this radical on the peptide, and (iv) the further attack of peptidyl radicals, formed following •OH attack.

2009 with permission from Elsevier). See also Colour Insert. , 2005). These three copper binding modes, classified as component 1, 2 and 3, have been widely characterized and are now well accepted. Component 1 is the main copper binding mode at high Cu2+ occupancy (2–4 Cu2+ equivalents) and it is characterized by copper coordination to each octapeptide unit (PHGGGWGQ) in a mode exactly coincident to Fig. 1. Component 2, dominating at intermediate Cu2+ occupancy (1–2 Cu2+ equivalents) is due to copper binding to one or two His imidazoles and to a deprotonated amide nitrogen.

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