| Alzheimer's disease(AD) is the most common form of dementia among aged population,which causes memory impairment and cognitive dysfunction and characterized by presence of extracellular fibrillar Aβin amyloid plaques,intraneuronal neurofibrillary tangles.At present,42-amino acid form of Aβsoluble oligomers (amyloidβ-protein) has been recognized as the pivotal impact factor in Alzheimer's disease.Abundant evidences suggest that the soluble Aβ1-42 oligomer has become the common target in the treatment of Alzheimer's disease.Here,the chemically synthetic Aβ1-42 oligomer has been assemblied in vitro.The resulted oligomer has been observed and assessed via SDS-PAGE,Western,ELISA and immunou blot assays.Our results showed that the profiles of this kind of oligomer appeared as a ladder in the molecular weight ranges from 4-170 kD,which were tetramer,hexamer and other higher moleculndar weight aggregations.In addition,there were still a little bit of monomer. The Aβ1-42 oligomer is stable in coating buffer and can be detected effectively in indirect ELISA.Immobilized Aβ1-42 oligomer on nitrocellulose filter could be recognized by monoclonal antibody 6E10 in immunoblot assays.Furthermore,the arrayed Aβ1-42 oligomer dots could be applied in fast and high throughput antibody detection and screenings.In conclusion,our results may provide important tools in Aβdetection,basic and therapeutic research in AD. |
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