Interactions between 1-benzoyl-4-p-chlorophenyl thiosemicarbazide and serum albumin: investigation by fluorescence spectroscopy

Cui, Fengling; Fan, Jing; Li, Jianping; Hu, Zhide

doi:10.1016/j.bmc.2003.10.018

Cited by 335 publications

(144 citation statements)

References 17 publications

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“…This indicates that 5-iodo-4-thio-2'-deoxyuridine binds with the amino acid residues of the main polypeptide chain of the protein and destroys their hydrogen bonding networks [28]. The results showed that 5-iodo-4-thio-2'-deoxyuridine role in the process of tumor cells by blood affect the structure of HSA is a small, there are extremely weak changes in the secondary structure of HSA.…”

Section: Investigation Of Conformational Changes On Binding Of 5-iodomentioning

confidence: 93%

Investigation on the Interaction of 5-iodo-4-thio-2’-deoxyuridine with Human Serum Albumin: Spectroscopic and Molecular Modeling Studies

Zhang¹,

Ling-shuang²

2015

Adv Tech Biol Med

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Section: Investigation Of Conformational Changes On Binding Of 5-iodomentioning

confidence: 93%

Investigation on the Interaction of 5-iodo-4-thio-2’-deoxyuridine with Human Serum Albumin: Spectroscopic and Molecular Modeling Studies

Zhang¹,

Ling-shuang²

2015

Adv Tech Biol Med

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“…As shown in Figure 5, the CD spectra of BSA exhibit two negative bands in the UV region at 209 and 222 nm, characteristic of the α-helical structure of the protein (24). The binding of Figure 3.…”

Section: Conformational Investigationsmentioning

confidence: 98%

Spectroscopic studies on the interaction of efonidipine with bovine serum albumin

Wang

Zhao

et al. 2008

Braz J Med Biol Res

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Efonidipine hydrochloride is an antihypertensive and antianginal agent with fewer side effects and is better tolerated in the treatment of hypertension with renal impairment. Its interaction with bovine serum albumin (BSA) is of great use for the understanding of the pharmacokinetic and pharmacodynamic mechanisms of the drug. The binding of efonidipine to BSA was investigated by fluorescence spectroscopy and circular dichroism. BSA fluorescence was quenched by efonidipine, due to the fact that efonidipine quenched the fluorescence of tryptophan residues mainly by the collision mode. The thermodynamic parameters ∆H 0 and ∆S 0 were 68.04 kJ/mol and 319.42 J·mol -1 ·K -1 , respectively, indicating that the hydrophobic interactions played a major role. The results of circular dichroism and synchronous fluorescence measurements showed that the binding of efonidipine to BSA led to a conformational change of BSA. The fraction of occupied sites (θ) for the 8-anilino-1-naphthaleinsulfonic acid (ANS)-BSA system is 85%, whereas for the NZ-105-BSA system, it is 53%, which suggests that the interaction of ANS with BSA is stronger than that of NZ-105 with BSA. Binding studies in the presence of ANS indicated that efonidipine competed with ANS for hydrophobic sites of BSA. The effects of metal ions on the binding constant of the efonidipine-BSA complex were also investigated. The presence of metal ions Zn 2+ , Mg 2+ , Al 3+ , K + , and Ca 2+ increased the binding constant of efonidipine-BSA complex, which may prolong the storage period of NZ-105 in blood plasma and enhance its maximum effects.

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“…30 Upon the addition of ergone, the a-helical content in protein was decreased, indicating that ergone bound with the amino acid residues of the main polypeptide chain of protein and destroyed their hydrogen bonding networks. 31 When the wavelength interval (Dl) between excitation wavelength and emission wavelength is 15 and 60 nm, the synchronous fluorescence spectra offer the characteristics of tyrosine and the tryptophan residues of HSA. 32 As seen from Fig.…”

Section: Conformation Investigationmentioning

confidence: 99%

Studies of Interaction between Ergosta‐4,6,8(14),22‐tetraen‐3‐one (Ergone) and Human Serum Albumin by Molecular Spectroscopy and Modeling

Sun

Zhao

et al. 2011

J Chinese Chemical Soc

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Our previous experimental results have shown that ergosta-4,6,8(14),22-tetraen-3-one (ergone) is one of the main bioactive components of Polyporus umbellatus. The efficacy of ergone binding to human serum albumin (HSA) is critical for pharmacokinetic behavior of ergone. The interactions between ergone and HSA under simulative physiological conditions were investigated by the methods of fluorescence spectroscopy, absorption and circular dichroism spectroscopy. Fluorescence data revealed that the fluorescence quenching of HSA by ergone was the result of the formation of the ergone-HSA complex. According to the modified Stern-Volmer equation, the binding constants (K a ) between ergone and HSA were determined. The thermodynamic parameters, enthalpy change (DH) and entropy change (DS) for the reaction were calculated to be 0.989 kJ mol -1 and 11.214 J mol -1 K -1 , indicating that the hydrogen bonds and hydrophobic interactions played a dominant role in the binding of ergone to HSA. The conformational investigation showed that the presence of ergone decreased the a-helical content of HSA and induced the slight unfolding of the polypeptides of protein. Furthermore, displacement experiments using warfarin and ibuprofen indicated that ergone could bind to site I of HSA, which was also in agreement with the results of the molecular modeling.

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Interactions between 1-benzoyl-4-p-chlorophenyl thiosemicarbazide and serum albumin: investigation by fluorescence spectroscopy

Cited by 335 publications

References 17 publications

Investigation on the Interaction of 5-iodo-4-thio-2’-deoxyuridine with Human Serum Albumin: Spectroscopic and Molecular Modeling Studies

Investigation on the Interaction of 5-iodo-4-thio-2’-deoxyuridine with Human Serum Albumin: Spectroscopic and Molecular Modeling Studies

Spectroscopic studies on the interaction of efonidipine with bovine serum albumin

Studies of Interaction between Ergosta‐4,6,8(14),22‐tetraen‐3‐one (Ergone) and Human Serum Albumin by Molecular Spectroscopy and Modeling

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