Localization of the noncovalent binding site between amyloid-beta-peptide and oleuropein using electrospray ionization FT-ICR mass spectrometry.
2008 (English)In: Journal of the American Society for Mass Spectrometry, ISSN 1044-0305, E-ISSN 1879-1123, Vol. 19, no 8, 1078-1085 p.Article in journal (Refereed) Published
Abnormal accumulation and aggregation of amyloid-alpha-peptide (AM) eventually lead to the formation and cerebral deposition of amyloid plaques, the major pathological hallmark in Alzheimer's disease (AD). Oleuropein (OE), an Olea europaea L. derived polyphenol, exhibits a broad range of pharmacological properties, such as antioxidant, anti-inflammatory, and antiatherogenic, which could serve as combative mechanisms against several reported pathways involved in the pathophysiology of AD. The reported noncovalent interaction between AM and OE could imply a potential antiamyloidogenic role of the latter on the former via stabilization of its structure and prevention of the adaptation of a toxic beta-sheet conformation. The established P-sheet conformation of the AM hydrophobic carboxy-terminal region and the dependence of its toxicity and aggregational propensity on its secondary structure make the determination of the binding site between AM and OF highly important for assessing the role of the interaction. In this study, two different proteolytic digestion protocols, in conjunction with high-sensitivity electrospray ionization mass spectrometric analysis of the resulting peptide fragments, were used to determine the noncovalent binding site of OE on AM and revealed the critical regions for the interaction.
Place, publisher, year, edition, pages
2008. Vol. 19, no 8, 1078-1085 p.
IdentifiersURN: urn:nbn:se:uu:diva-149505DOI: 10.1016/j.jasms.2008.03.011ISI: 000258538500006PubMedID: 18448354OAI: oai:DiVA.org:uu-149505DiVA: diva2:405093
Conference Information: DESORPTION 2006 Meeting
Goulandris Nat Hist Museum, Kifissia, GREECE, SEP 03-07, 2006 2011-03-212011-03-202011-03-22Bibliographically approved