Studies on the binding of nevadensin to human serum albumin by molecular spectroscopy and modeling

Li, Daojin; Zhu, Jingfeng; Jin, Jing; Yao, Xiaojun

doi:10.1016/j.molstruc.2007.01.020

Cited by 129 publications

(58 citation statements)

References 30 publications

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“…As shown in Table 5, the a-helical content of HSA slightly decreases at temperature from 298-310 K that is from 58.83 to 57.41 %, while the a-helical content of HSA increases on addition of AX amount from 0 to 25 lM. It can be concluded that occupancy of the tryptophan sites by the binding ligands actually could stabilize the native conformation of protein [13]. This result indicates that HSA is predominantly a-helix in nature even after binding to the drug.…”

Section: Spectra Studiesmentioning

confidence: 84%

“…The midpoint temperature (T m ) was determined by fitting the ellipticity values into a two-state folding-unfolding model Eqs. (12) and (13), and DG°v alues have been determined by Eqs. (14) and (15).…”

Section: Effect Of Ax On Thermal Stability Of Hsamentioning

confidence: 99%

“…The investigation of the interaction of HSA with drugs contributes to understand disposition, transportation, metabolism and efficacy of drugs, which are correlated with their affinities toward HSA. Therefore, it is of great importance to study the binding of drugs to HSA [13]. The binding of ligands to proteins occurs mostly through noncovalent interactions, namely hydrophobic interaction, van der Waals forces, and hydrogen bonding in low dielectric medium [14].…”

Section: Introductionmentioning

confidence: 99%

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Calorimetric and spectroscopic binding studies of amoxicillin with human serum albumin

Yasmeen

Riyazuddeen

Rabbani

2016

J Therm Anal Calorim

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Amoxicillin is a common antibiotic drug used for preventing bacterial colonization of urinary and skin infections. The binding of amoxicillin (AX) to human serum albumin (HSA) in sodium phosphate buffer solution at pH 7.4 has been investigated by UV-visible spectroscopy, fluorescence spectroscopy, Förster resonance energy transfer, isothermal titration calorimetry (ITC), circular dichroism (CD) and FTIR spectroscopy. The binding studies using ITC revealed that the interaction is entropy driven rather than enthalpy as the change in enthalpy (DH°) and change in entropy (TDS°) both are positive, indicating the endothermic reaction with low affinity and hydrophobic interaction. UV-visible absorption spectra of HSA are increased upon addition of AX which shows complex formation of HSA-AX. The fluorescence spectra reveal that the AX has an ability to quench the intrinsic fluorescence of HSA tryptophan through a static quenching procedure. The molecular distance r between donor (HSA) and acceptor (AX) was estimated according to Förster theory of nonradiative energy transfer. The CD spectra showed that the a-helix of HSA increases with increasing the amount of AX. The thermal denaturation has been studied by far-UV CD, and it is found that HSA stability is decreased by the complex formation of HSA and AX. The remarkable change in amide I peak position in infrared spectrum after interaction with AX indicated that secondary structure of HSA has been changed.

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Section: Spectra Studiesmentioning

confidence: 84%

Section: Effect Of Ax On Thermal Stability Of Hsamentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Calorimetric and spectroscopic binding studies of amoxicillin with human serum albumin

Yasmeen

Riyazuddeen

Rabbani

2016

J Therm Anal Calorim

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“…Then, the binding distance r between Co(phen) 3 2+ and BSA may be as close as 4.11 nm. The donor-to-acceptor distance r is less than 8 nm, indicating that the energy transfer from BSA to Co(phen) 3 2+ occurred with high possibility [30].…”

Section: Number Of Binding Sites and Identification Of The Binding Lomentioning

confidence: 99%

Spectroscopic Studies on the Binding of Cobalt(II) 1,10-Phenanthroline Complex to Bovine Serum Albumin

Zhang

Dai

et al. 2009

Biol Trace Elem Res

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The binding interaction of the cobalt(II) 1,10-phenanthroline complex (Co(phen) (3) (2+) , phen = 1,10-phenanthroline) with bovine serum albumin (BSA) was investigated by fluorescence spectroscopy combined with UV-Vis absorption and circular dichroism measurements under simulative physiological conditions. The experiment results showed that the fluorescence intensity of BSA was dramatically decreased owing to the formation of Co(phen) (3) (2+) -BSA complex. The corresponding association constants (K (a)) between Co(phen) (3) (2+) and BSA at four different temperatures were calculated according to the modified Stern-Volmer equation. The enthalpy change (DeltaH degrees ) and entropy change (DeltaS degrees ) were calculated to be -2.73 kJ mol(-1) and 82.27 J mol(-1) K(-1), respectively, which suggested that electrostatic interaction and hydrophobic force played major roles in stabilizing the Co(phen) (3) (2+) -BSA complex. Site marker competitive experiments indicated that the binding of Co(phen) (3) (2+) to BSA primarily took place in site I of BSA. A value of 4.11 nm for the average distance r between Co(phen) (3) (2+) (acceptor) and tryptophan residues of BSA (donor) was derived from Förster's energy transfer theory. The conformational investigation showed that the presence of Co(phen) (3) (2+) resulted in the change of BSA secondary structure and induced the slight unfolding of the polypeptides of protein, which confirmed the microenvironment and conformational changes of BSA molecules.

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“…When the wavelength interval (Dl) was fixed at 60 nm of protein, the synchronous fluorescence had the same intensity as the emission fluorescence following excitation at 280 nm, and just the emission maximum wavelength and shape of the peaks changed. [21][22][23] Thus, the synchronous fluorescence measurements can be applied to calculate association constants similar to the emission fluorescence measurements. Therefore, the synchronous fluorescence measurements can deduce the binding mechanism as the emission fluorescence measurements did.…”

Section: Characteristics Of Synchronous Fluorescence Methodsmentioning

confidence: 99%

Study of the Interaction of Aglycon of Daunorubicin with Human Serum Albumin by Spectroscopy and Modeling

Cui

Qin

Zhang

et al. 2008

Macromolecular Bioscience

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The interaction between aglycon of daunorubicin (DNR-A) and human serum albumin (HSA) was investigated using fluorescence quenching and modeling. Results shown that fluorescence quenching of HSA by DNR-A resulted from the formation of DNR-A-HSA complex. The quenching constants were determined via measurement of the binding affinity between DNR-A and HSA using the Stern-Volmer equation. The thermodynamic parameters DeltaG, DeltaH, DeltaS and the binding distance r were calculated. Furthermore, SFS and UV spectra suggested that the complex changed the conformation of HSA and that hydrophobic interactions played a major role in DNR-A-HSA association, which was in good agreement with the results of the modeling study. Moreover, the SFS technique was successfully applied to determine the total proteins in biology samples with satisfactory results.

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Studies on the binding of nevadensin to human serum albumin by molecular spectroscopy and modeling

Cited by 129 publications

References 30 publications

Calorimetric and spectroscopic binding studies of amoxicillin with human serum albumin

Calorimetric and spectroscopic binding studies of amoxicillin with human serum albumin

Spectroscopic Studies on the Binding of Cobalt(II) 1,10-Phenanthroline Complex to Bovine Serum Albumin

Study of the Interaction of Aglycon of Daunorubicin with Human Serum Albumin by Spectroscopy and Modeling

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