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Biochim Biophys Acta. 2008 Dec;1784(12):2052-8. PubMed; doi 10.1016/j.bbapap.2008.07.013

Non-native glyceraldehyde-3-phosphate dehydrogenase can be an intrinsic component of amyloid structures.

Naletova, I.; Schmalhausen, E.; Kharitonov, A.; Katrukha, A.; Saso, L.; Caprioli, A.; Muronetz, V.

Interactions between different forms of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and amyloid-beta peptide (1-42) were investigated by direct (surface plasmon resonance) and indirect (kinetics of spontaneous and GroEL/S-assisted reactivation of denatured GAPDH) methods. It was demonstrated that non-native forms of GAPDH obtained by different ways (cold denaturation, oxidation of the enzyme, and its unfolding in guanidine hydrochloride) efficiently bind to soluble amyloid-beta peptide (1-42) yielding a stable complex. Native tetrameric GAPDH does not interact with soluble amyloid-beta peptide (1-42), neither non-native forms of GAPDH interact with aggregated amyloid-beta peptide (1-42). The results suggest that non-native GAPDH species can be involved in the formation of amyloid structures during Alzheimer's disease, binding to soluble amyloid-beta peptide (1-42).



 


  Московский Государственный Университет имени М.В.Ломоносова



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