Studies on the role of amino acid stereospecificity in amyloid beta aggregation.
Amyloid beta (Abeta) deposition and neurodegeneration are the two related events in the pathogenesis of Alzheimer's disease. Several factors modulate the conformation and physical properties of Abeta, which in turn affects its biological functions. Among these, age-dependent changes in the stereospecificity of the amino acids comprising Abeta is one such factors. In the present study, we investigated the aggregation property of Abeta as a function of the stereospecificity of amino acids comprising the peptide. We carried out our study by comparing the physical properties of Abeta(1-40) all-L and Abeta(1-40) all-D enantiomers using various biophysical techniques. These results indicated that the aggregation and folding parameters of Abeta are stereospecific and the aggregation property strongly depends upon the amino acid sequence and their stereospecificity. This may possibly help to understand the stereospecific role of amino acids comprising Abeta in its aggregation and its relevance to neurodegeneration.
D000375:Aging / Q000378:metabolism / Q000473:pathology; D000544:Alzheimer Disease / Q000378:metabolism* / Q000503:physiopathology; D000595:Amino Acid Sequence / Q000502:physiology; D000596:Amino Acids / Q000737:chemistry*; D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D002479:Inclusion Bodies / Q000378:metabolism; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D058225:Plaque, Amyloid / Q000378:metabolism*; D011487:Protein Conformation; D017510:Protein Folding; D013237:Stereoisomerism
D000596:Amino Acids; D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; C078592:amyloid beta-protein (1-40)