Competitive binding of Chlorin p6 and Dansyl-l-Proline to Sudlow’s site II of human serum albumin

Patel, Sunita; Sharma, Kaushal; Datta, Anindya

doi:10.1016/j.saa.2014.10.015

Cited by 17 publications

(14 citation statements)

References 42 publications

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“…They are located in the hydrophobic cavities of the molecule, subdomain IIA and IIIA, respectively [6]. A few years later Yamasaki et al proposed novel nomenclatures for binding site I: regions Ia, Ib and Ic [7]. Binding region of phenylbutazone corresponds to the region Ia and Ib.…”

Section: Introductionmentioning

confidence: 99%

Human Serum Albumin Aggregation/Fibrillation and its Abilities to Drugs Binding

et al. 2020

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Human serum albumin (HSA) is a protein that transports neutral and acid ligands in the organism. Depending on the environment’s pH conditions, HSA can take one of the five isomeric forms that change its conformation. HSA can form aggregates resembling those in vitro formed from amyloid at physiological pH (neutral and acidic). Not surprisingly, the main goal of the research was aggregation/fibrillation of HSA, the study of the physicochemical properties of formed amyloid fibrils using thioflavin T (ThT) and the analysis of ligand binding to aggregated/fibrillated albumin in the presence of dansyl-l-glutamine (dGlu), dansyl-l-proline (dPro), phenylbutazone (Phb) and ketoprofen (Ket). Solutions of human serum albumin, both non-modified and modified, were examined with the use of fluorescence, absorption and circular dichroism (CD) spectroscopy. The experiments conducted allowed observation of changes in the structure of incubated HSA (HSAINC) in relation to nonmodified HSA (HSAFR). The formed aggregates/fibrillation differed in structure from HSA monomers and dimers. Based on CD spectroscopy, previously absent β-structural constructs have been registered. Whereas, using fluorescence spectroscopy, the association constants differing for fresh and incubated HSA solutions in the presence of dansyl-amino acids and markers for binding sites were calculated and allowed observation of the conformational changes in HSA molecule.

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Section: Introductionmentioning

confidence: 99%

Human Serum Albumin Aggregation/Fibrillation and its Abilities to Drugs Binding

et al. 2020

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“…Supramolecular binding of the hexacarboxyl-terminated iron(II) clathrochelates to BSA and HSA BSA and HSA are heart-shaped proteins, the crystal structures of which are very similar. 41 The molecule of HSA consists of three helical domains (I, II and III), each comprising two subdomains (A and B; Fig. 1).…”

Section: Resultsmentioning

confidence: 99%

“…49,50 Apart from Trp, also tyrosine (Tyr) residues contribute to the intrinsic fluorescence of proteins; 51 BSA and HSA contain twenty and eighteen Tyr residues per protein macromolecule, respectively. 2,41 However, in comparison to Trp, the fluorescence of Tyr residues is less intense and independent of the local environment.…”

Section: Resultsmentioning

confidence: 99%

“…Thus, a significantly higher percentage of clathrochelate molecules is bound to albumins at a 2 : 1 molar ratio for the conditions of the CD experiment, and induced CD was clearly observed. The clathrochelate binding site was evaluated by displacement of clathrochelate upon addition of site markers: (i) warfarin, 3,41 and (ii) ibuprofen. 13 A 50-fold excess (2 Â 10 À3 M) of warfarin or ibuprofen was added to a mixture of protein (c albumin = 8 Â 10 À5 mol l À1 ) and clathrochelate (c clt = 4 Â 10 À5 mol l À1 ).…”

Section: Icd Spectroscopymentioning

confidence: 99%

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Induced CD of iron(ii) clathrochelates: sensing of the structural and conformational alterations of serum albumins

et al. 2019

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“…Protein binding refers to the ability of a drug molecule to interact with proteins through reversible or irreversible processes. The biological properties of a drug are highly dependent on its ability to bind to protein, which has important roles in enzymatic action, hormone activity, genic regulation and drug transport . Because of this, probing the protein‐binding properties of AZN is of great significance.…”

Section: Introductionmentioning

confidence: 99%

Comparison and analysis on the serum‐binding characteristics of aspirin–zinc complex and aspirin

Zhang

Wang

et al. 2017

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This study was designed to compare the protein-binding characteristics of aspirin-zinc complex (AZN) with those of aspirin itself. AZN was synthesized and interacted with a model transport protein, human serum albumin (HSA). Three-dimensional fluorescence, ultraviolet-visible and circular dichroism (CD) spectra were used to characterize the interaction of AZN with HSA under physiological conditions. The interaction mechanism was explored using a fluorescence quenching method and thermodynamic calculation. The binding site and binding locality of AZN on HSA were demonstrated using a fluorescence probe technique and Förster non-radiation energy transfer theory. Synchronous fluorescence and CD spectra were employed to reveal the effect of AZN on the native conformation of the protein. The HSA-binding results for AZN were compared with those for aspirin under consistent experimental conditions, and indicated that aspirin acts as a guide in AZN when binding to Sudlow's site I, in subdomain IIA of the HSA molecule. Moreover, compared with aspirin, AZN showed greater observed binding constants with, but smaller changes in the α-helicity of, HSA, which proved that AZN might be easier to transport and have less toxicity in vivo.

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Competitive binding of Chlorin p6 and Dansyl-l-Proline to Sudlow’s site II of human serum albumin

Cited by 17 publications

References 42 publications

Human Serum Albumin Aggregation/Fibrillation and its Abilities to Drugs Binding

Human Serum Albumin Aggregation/Fibrillation and its Abilities to Drugs Binding

Induced CD of iron(ii) clathrochelates: sensing of the structural and conformational alterations of serum albumins

Comparison and analysis on the serum‐binding characteristics of aspirin–zinc complex and aspirin

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