Preparation of artificial receptors for beta-amyloid protein by hierarchical imprinting techniques.

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Alzheimer s disease (AD) is the most common form of dementia in humans. Recent researchsuggests that the deposition of cerebral amyloid plaques is central to the disease process.Amyloid deposits mainly comprise aggregates of ß-amyloid (Aß), a 38-43 amino acid peptidederived by proteolytic cleavage of the amyloid precursor protein (APP). The larger peptides(42-43 amino acid residues) are theorised to be more potent towards aggregation and, thus,plaque formation and neuronal death. Therefore, there is an increased interest in theseparation and differentiation between the several amyloid forms. Conventional separationtechniques or immunoassays have so far shown less promise for such purposes due toinsufficient selectivity, high cost or difficulties in production. Artificial receptors for Aß-peptideswill be manufactured utilising a previously developed surface imprinting technique(see DFG SE 777/5-1), This uses crude solid phase peptide synthesis products (shortsequences of < 5 amino acids) as templates to generate epitope-imprinted surfaces inmesoporous polymer beads. The beads will be targeted to exhibit recognition of the N- or C-terminalsequences of the target peptide. The entire peptide, including the varying terminals(40, 41, 42, 43 residues), will be targeted and the resulting beads assessed for their ability toselectively extract and enrich the Aß variants from cerebrospinal fluid (CSF) or blood plasmafor analytical (diagnostic) or therapeutic (blood treatment) purposes.