Literature DB >> 19385598

Amyloid beta protein: Abeta40 inhibits Abeta42 oligomerization.

Megan M Murray1, Summer L Bernstein, Vy Nyugen, Margaret M Condron, David B Teplow, Michael T Bowers.   

Abstract

Abeta40 and Abeta42 are peptides that adopt similar random-coil structures in solution. Abeta42, however, is significantly more neurotoxic than Abeta40 and forms amyloid fibrils much more rapidly than Abeta40. Here, mass spectrometry and ion mobility spectrometry are used to investigate a mixture of Abeta40 and Abeta42. The mass spectrum for the mixed solution shows the presence of a heterooligomer composed of equal parts of Abeta40 and Abeta42. Ion mobility results indicate that this mixed species comprises an oligomer distribution extending to tetramers. Abeta40 alone produces such a distribution, whereas Abeta42 alone produces oligomers as large as dodecamers. This indicates that Abeta40 inhibits Abeta42 oligomerization.

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Year:  2009        PMID: 19385598      PMCID: PMC2697393          DOI: 10.1021/ja8092604

Source DB:  PubMed          Journal:  J Am Chem Soc        ISSN: 0002-7863            Impact factor:   15.419


  14 in total

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5.  Abeta40 protects non-toxic Abeta42 monomer from aggregation.

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  51 in total

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Review 7.  Abeta, oxidative stress in Alzheimer disease: evidence based on proteomics studies.

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8.  Factors that influence helical preferences for singly charged gas-phase peptide ions: the effects of multiple potential charge-carrying sites.

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