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and then excited with a laser to emit light of a different wavelength, which was captured by a detector and generated as an image/graph.
Since we were sure of osteocalcin and Abeta42 association, we were curious whether these conferred any protection. Therefore, we performed an experiment in which an increased concentration of osteocalcin was exposed to a constant concentration of Abeta42 in a tube to evaluate whether any concentration of osteocalcin (undercarboxylated form) reduced the toxicity of Abeta42 by A11 immunoblotting. Thetechniqueusedanantibodythatidentified a specific conformation shown only by pathogenic peptides such as prion, synuclein, etc. We identified that osteocalcin bound to Abeta42 and reduced its toxicity that led to the development of a novel A-O complex (A for Abeta and O for osteocalcin), which was a heterogeneous mixture of hydrated structures and immature fibrils visualized using atomic force microscopy (AFM). AFM was a different form of advanced microscopy where a ‘tip’
Dr Viji Vijayan || 63
was used as a mechanical probe to scan the structure of the specimen, magnify surface features up to 100,000 times and thus produce a 3D image without any staining procedures. A-O was discovered to possess immunomodulatory activities as evidenced by its ability to reduce inflammatory markers and modulate markers on cell-eating phagocytic cells such as ‘macrophages’. A-O had the potential to stimulate and take up pathogenic peptides like not only Abeta42 but also other ligands such as oxidative low-density-lipoprotein that caused cardiovascular complications. The National Institute of Immunology has sought patent protection for the A-O complex, and we hope that this peptide-therapeutic composed of integral body components had beneficial effects on the body and would be the future of the Alzheimer disease therapy. Our research gives out the message that a bone is an organ that needs special protection in all the phases of our lives.