Binding (Kb) and quenching constant (Kq) data and the number of binding sites (n) of BSA interaction with the titled compoundsa.
| Absorption spectroscopy λmax = 278 nm | Emission spectroscopy λmax = 345 nm | ||||||
|---|---|---|---|---|---|---|---|
| Compound | (Kb), × 104 | % hyper | % hypo | (Ksv), × 104 | (Kq), × 1012 | (Kb) | n |
| HL | 1.0 | 39.03 | 27.18 | 2.33 | 2.33 | 8.9 × 103 | 0.93 |
| (C1) | 4.6 | 36.05 | 69.44 | 5.68 | 5.68 | 4.0 × 105 | 1.61 |
| (C2) | 2.5 | 11.90 | 42.63 | 5.39 | 5.39 | 3.9 × 104 | 1.03 |
| (C3) | 1.52 | 40.74 | 35.69 | 4.98 | 4.98 | 2.6 × 104 | 0.92 |
a
The observed BSA binding constant (K) values for all the compounds are presented in (2). It was found that the C1 complex exhibited the highest binding strength with BSA in the order of C1 > C2 > C3 > HL.