Interaction Study between ESIPT Fluorescent Lipophile-Based Benzazoles and BSA
In this study, the interactions of ESIPT fluorescent lipophile-based benzazoles with bovine serum albumin (BSA) were studied and their binding affinity was evaluated. In phosphate-buffered saline (PBS) solution these compounds produce absorption maxima in the UV region and a main fluorescence emissi...
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| Autores principales: | , , , , , , , |
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| Formato: | article |
| Lenguaje: | EN |
| Publicado: |
MDPI AG
2021
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| Materias: | |
| Acceso en línea: | https://doaj.org/article/4afa70aac0f444d6b76cadc99187c828 |
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| Sumario: | In this study, the interactions of ESIPT fluorescent lipophile-based benzazoles with bovine serum albumin (BSA) were studied and their binding affinity was evaluated. In phosphate-buffered saline (PBS) solution these compounds produce absorption maxima in the UV region and a main fluorescence emission with a large Stokes shift in the blue–green regions due to a proton transfer process in the excited state. The interactions of the benzazoles with BSA were studied using UV-Vis absorption and steady-state fluorescence spectroscopy. The observed spectral quenching of BSA indicates that these compounds could bind to BSA through a strong binding affinity afforded by a static quenching mechanism (K<sub>q</sub>~10<sup>12</sup> L·mol<sup>−1</sup>·s<sup>−1</sup>). The docking simulations indicate that compounds <b>13</b> and <b>16</b> bind closely to Trp134 in domain I, adopting similar binding poses and interactions. On the other hand, compounds <b>12</b>, <b>14</b>, <b>15</b>, and <b>17</b> were bound between domains I and III and did not directly interact with Trp134. |
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