2022
DOI: 10.1039/d1ra07195e
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Deciphering the sensing of α-amyrin acetate with hs-DNA: a multipronged biological probe

Abstract: In this study, we focus on the biomimetic development of small molecules and their biological sensing with DNA.

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Cited by 5 publications
(4 citation statements)
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“…The 1 H and 13 C NMR spectra of the QRT were recorded at 500 mHz ( 1 H NMR) and 125 mHz (13C NMR) using the Bruker (Advance) NMR instrument in DMSO solvent. 41 1 H NMR (500 MHZ, DMSO- d 6 ): δ 6.18 (d, 1H, J = 2 Hz), 6.40 (d, 1H, J = 1.5 Hz), 6.87 (d, 1H, J = 9 Hz), 7.52 (dd, 1H, J = 2.5 and 8.5 Hz), and 7.67 (d, 1H, J = 2.5 Hz). 13 C NMR (125 MHZ, DMSO- d 6 ): δ 93.32, 98.15, 102.98, 115.03, 115.57, 119.94, 121.92, 135.70, 145.03, 146.77, 147.67, 156.11, 160.69, 163.85, and 175.81.…”
Section: Methodsmentioning
confidence: 99%
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“…The 1 H and 13 C NMR spectra of the QRT were recorded at 500 mHz ( 1 H NMR) and 125 mHz (13C NMR) using the Bruker (Advance) NMR instrument in DMSO solvent. 41 1 H NMR (500 MHZ, DMSO- d 6 ): δ 6.18 (d, 1H, J = 2 Hz), 6.40 (d, 1H, J = 1.5 Hz), 6.87 (d, 1H, J = 9 Hz), 7.52 (dd, 1H, J = 2.5 and 8.5 Hz), and 7.67 (d, 1H, J = 2.5 Hz). 13 C NMR (125 MHZ, DMSO- d 6 ): δ 93.32, 98.15, 102.98, 115.03, 115.57, 119.94, 121.92, 135.70, 145.03, 146.77, 147.67, 156.11, 160.69, 163.85, and 175.81.…”
Section: Methodsmentioning
confidence: 99%
“…The 1 H and 13 C NMR spectra of the QRT were recorded at 500 mHz ( 1 H NMR) and 125 mHz (13C NMR) using the Bruker (Advance) NMR instrument in DMSO solvent. 41 1 H NMR (500 MHZ, DMSO-d 6 ): d 6.18 (d, 1H, J ¼ 2 Hz), 6.40 (d, 1H, J ¼ 1.5 Hz), 6.87 (d, 1H, J ¼ 9 Hz), 7.52 (dd, 1H, J ¼ 2.5 and 8.5 Hz), and 7.67 (d, 1H, J ¼ 2.5 Hz). 13…”
Section: Characterizations Of Small Molecule Qrtmentioning
confidence: 99%
“…33 Three modules were found for the binding of small molecules to the DNA double helix; intercalative, groove, and electrostatic binding. 34,35…”
Section: Introductionmentioning
confidence: 99%
“…33 Three modules were found for the binding of small molecules to the DNA double helix; intercalative, groove, and electrostatic binding. 34,35 The presence of structural homology between bovine serum albumin (BSA) and human serum albumin (HSA) 36 leads to the interaction between BSA and drug molecules that forms a vital fundamental issue in life science. Drugs binding to the proteins present in the blood stream is a vital process to determine their eventual activities in the circulatory system.…”
Section: Introductionmentioning
confidence: 99%