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| AptBacDB_ID ⇅ | PMID/DOI ⇅ | Year ⇅ | Title ⇅ | Aptamer name ⇅ | Sequence (5′ to 3′) ⇅ | Length ⇅ | Library ⇅ | Type ⇅ | Target Organism ⇅ | Target ⇅ | Objective/Mechanism ⇅ | Outcome/Inhibitory effect ⇅ | No. of selection round SELEX ⇅ | Determination of affinity method ⇅ | Kd value ⇅ | Activity Role ⇅ | Method ⇅ | Modification ⇅ | Cytotoxicity (cell viability) ⇅ | Stability⇅ | Potential Candidate ⇅ | Half-life ⇅ | Patent ⇅ |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| ABdb_0058 | 19751419 | 2009 | Antibiotic resistance in bacteria: novel metalloenzyme inhibitors | Metallo-β-lactamase-targeting aptamers | CGCGAGCTCCGCGCG-AACCAAACTTGGATCGGTGCACATGTCGAA-CGCGCGCATATGGCGC | 61 | 5'-CGCGAGCTCCGCGCG-N30-CGCGCGCATATGGCGC-3' | ssDNA | Bacillus Cereus 5/B/6 and Escherichia Coli (E. Coli) TAP56 | Metallo-β-lactamase active sites | Identify aptamers that bind and inhibit the hydrolytic enzyme activity by interfering with the active-site metal ions of the β-lactamase enzyme. | LC50 values in the presence of 5 μM cephalexin: 75 μM and 32 μM for B. cereus 5/B/6 and E. coli TAP56, respectively. | 21 | Metallo-β-lactamase activity assays | Ki = 0.92 nM | Therapeutics | SELEX | N/A | N/A | N/A | N/A | N/A | N/A |