Surface tension and intrinsic amyloid fluorescence of serum and cerebrospinal fluid samples in Alzheimeŕs disease

Abstract

Aim: Surface tension of biological fluids can be influenced by changes in oligomerization or aggregation of surfactant peptides or proteins. Amphiphilic peptides of amyloid-β or other amyloidogenic peptides/proteins display properties of surfactants, oligomerization and aggregation increase also their fluorescence intensity compared with native structures. Results/methodology: We estimated surface tension and native/ThioflavinT-based/intrinsic amyloid fluorescence intensity in serum and cerebrospinal fluid samples for their evalution as diagnostic biomarkers for Alzheimeŕs disease (AD). Discussion/conclusion: Our results indicate that values of surface tension are not a suitable biomarker for AD. However, the ratio of ThioflavinT-based fluorescence to intrinsic amyloid fluorescence in cerebrospinal fluid appears to be an acceptable supportive diagnostic biomarker for AD (its sensitivity was 61.1%, and the specificity 70.8% when compared with aged controls).