The unique solvatochromic attitude of an analyte owing
to its coordination
with metal ions in solvents of different polarities is challenging.
Herein, we introduce two new solvatochromic 4-(pentan-3-yl) benzaldehyde-based
triazolyl silatrane probes (5 and 6). The
solvatochromic behavior of both probes 5 and 6 was studied using Reichardt’s E (30) and the Kamlet–Taft
empirical scale by UV–visible spectra in 14 solvents (hydrogen-bond
donor (HBD) and non-HBD), and the results show that probes 5 and 6 exhibit reverse solvatochromism. Probe 5 witnessed an enhancement in this behavior upon coordination
with the Cu2+ ion in MeCN/MeOH solvents due to the intramolecular
charge transfer (ICT) process. Interestingly, the binding of probe 5 with Cu2+ ions resulted in an instant color change
in MeCN and MeOH from pale yellow to light blue and brown-red, respectively,
which can be easily detected by the “naked eye”. A solvatochromic
study of the complex 5–Cu2+ in binary
mixtures of polar aprotic and polar protic solvents (MeCN/MeOH) discloses
that the latter are more preferred over polar aprotic solvents in
the solvation microsphere. The entire metal coordination process of
probe 5 toward the Cu2+ ion can be visualized
and was further evaluated by UV–vis/fluorescence spectral titrations,
Fourier transform infrared (FT-IR) spectroscopy, and theoretical calculations
employing density functional theory (DFT) and time-dependent-DFT (TD-DFT).
The proposed analytical approach is believed to play a crucial role
in the solvatochromic study of higher coordinated silicon compounds,
which may be utilized to develop a solvent-dependent sensor.
In the present investigation, the protein-binding properties of naphthyl-based hydroxamic acids (HAs), N-1-naphthyllaurohydroxamic acid (1) and N-1-naphthyl-pmethylbenzohydroxamic acid (2) were studied using bovine serum albumin (BSA) and UV-visible spectroscopy, fluorescence spectroscopy, diffuse reflectance spectroscopy-Fourier transform infrared (DRS-FTIR), circular dichroism (CD), and cyclic voltammetry along with computational approaches, i.e. molecular docking.Alteration in the antioxidant activities of compound 1 and compound 2 during interaction with BSA was also studied. From the fluorescence studies, thermodynamic parameters such as Gibb's free energy (ΔG), entropy change (ΔS) and enthalpy change (ΔH) were calculated at five different temperatures (viz., 298, 303, 308, 313 or 318 K) for the HAs-BSA interaction. The results suggested that the binding process was enthalpy driven with dominating hydrogen bonds and van der Waals' interactions for both compounds. Warfarin (WF) and ibuprofen (IB) were used for competitive site-specific marker binding interaction and revealed that compound 1 and compound 2 were located in subdomain IIA (Sudlow's site I) on the BSA molecule. Conclusions based on above-applied techniques signify that various non-covalent forces were involved during the HAs-BSA interaction. Therefore the resulted HAs-BSA interaction manifested its effect in transportation, distribution and metabolism for the drug in the blood circulation system, therefore establishing HAs as a drug-like molecule. KEYWORDS bovine serum albumin (BSA), circular dichroism, fluorescence spectroscopy, molecular docking, naphthylhydroxamic acids
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