Part:BBa_K4397004:Design
Amyloid-Beta - 7-92-1H1
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Design Notes
(Zheng et al., 2022) obtained three Aβ42 monomer-specific DNA aptamers based on magnetic bead-assisted in vitro screening [77]. Moreover, DNA aptamer Aβ7-92-1H1 with a length of 44 bases was obtained through further sequence optimization. DNA aptamer Aβ7-92-1H1 possessed the stem-loop structure. Besides, the Kd value of the aptamer binding to the Aβ42 monomer is 63.4 nM, which also showed high specificity of this aptamer for Aβ42 monomer moreovoer two peptide aptamers (c-abp2 and n-abp4) were confirmed to have excellent binding affinity to Aβ aggregates with high specificity (Rahimi et al.) obtained RNA aptamers (KM33 and KM41) using Aβ40 oligomer as the target by nitrocellulose membrane filtration method [75]. However, these RNA aptamers did not recognize Aβ40 oligomer but bound to Aβ40 fibril, Aβ42 fibril and other types of amyloid fibrils (such as lysozyme amyloid fibril, islet amyloid fibril, etc.) (Tsukakoshi et al.) obtained 8 DNA aptamers bound to α-synuclein oligomers based on a competitive screening method
Source
Genomic Sequence