The Structure-Activity Relationship of Glycosaminoglycans and Their Analogues with β-Amyloid Peptide

Alzheimer's disease (AD) is a serious neurodegenerative disorder. beta-amyloid peptide (A beta) aggregation is believed to be the major cause of the disease. The process of A beta aggregation can be enhanced by sulfated glycosaminoglycans. However, cell experiments have shown that sulfated glycosaminoglycan oligosaccharides or analogues may have significant neuroprotective properties and could inhibit the aggregation by competitive inhibition. The length and species of oligosaccharides or analogues can inhibit the toxicity of A beta by inducing conformational changes of proteins in different manners. This review presents the conformational changes of A beta in the presence of glycosaminoglycan, glycosaminoglycan oligosaccharides and analogues. The review might be helpful to comprehend the mechanism of beta-amyloid fibrillations and the aggregation process.