Cadmium(II), zinc(II), and copper(II) ions binding to bovine serum albumin. A 113Cd NMR study

Martins, E.; Drakenberg, Torbjörn

doi:10.1016/s0020-1693(00)85042-2

Cited by 55 publications

(32 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The binding of ions to the polar groups of amphiphilic compounds is a subject of continuing interest and of great importance in various areas of chemistry and biochemistry (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12). Unfortunately, as is often the case with biological systems, studies are hampered by the extreme complexity of the system being studied.…”

Section: Introductionmentioning

confidence: 99%

The interactions of the chloride and bromide ions in nematic lyotropic liquid crystalline solution

Tracey¹

1984

Can. J. Chem.

View full text Add to dashboard Cite

ALAN S . TRACEY. Can. J. Chem. 62, 2161Chem. 62, (1984.The binding interactions of chloride and bromide ions have been studied in nematic lyotropic liquid crystalline materials prepared using the mixed detergent system of potassium dodecanoate/dodecylpyridinium chloride. The results from this study show that a three-site model of binding is sufficient to describe the behaviour of the observed quadrupole splittings. The results clearly reveal that the selectivity of ion binding is a function not only of the counterion but also of the detergent ion to which it is bound. In the cationic mesophase prepared from decylpyridinium, Cl-binds simultaneously to two and Br-to three headgroups. This contrasts with the alkyltrimethylammonium bromide system, where Cl-binds to three cationic amphiphiles while Br-binds to two. Sodium ion appears indifferent to the type of cationic detergent present, a result in accordance with the expectation that its binding is determined only by the headgroup of the anionic detergent. Extension of the three-site theory to take into account the effect of surface charge on ion binding provides information concerning relative strengths of binding. In the dodecylpyridinium system CI-binds only weakly compared to Br-whereas in the alkyltrimethylammonium system Clbinds more strongly than Br-. K' binds most strongly to dodecanoate anion, CsC least strongly, and the other alkali metal ions occupy intermediate positions. IntroductionThe binding of ions to the polar groups of amphiphilic compounds is a subject of continuing interest and of great importance in various areas of chemistry and biochemistry (1-12). Unfortunately, as is often the case with biological systems, studies are hampered by the extreme complexity of the system being studied. For the particular case of ion binding a further impediment often encountered is that the details of the stereochemical requirements which are imposed on a substrate by the ion during binding interactions are not known. A study of simple systems can often provide the background information necessary for understanding the more complex systems.A particularly suitable medium for studying ion interactions is that of lyotropic liquid crystals. Of these materials, those which have the property of spontaneously aligning in the magnetic field of a nuclear magnetic resonance spectrometer provide distinct advantages, the most important one being "sharp" nrnr transitions, which result from the fact that the mesophase directors are aligned homogeneously by the magnetic field of the spectrometer (1 3).Of particular utility in the study of ion binding is the mixed detergent system prepared from potassium dodecanoate (potassium laurate) and alkyltrimethylammonium bromide. This system has the advantage in that, under the appropriate conditions, the potassium dodecanoate can be replaced in a stepwise fashion by alkyltrimethylammonium bromide, thus progressing

show abstract

Section: Introductionmentioning

confidence: 99%

The interactions of the chloride and bromide ions in nematic lyotropic liquid crystalline solution

Tracey¹

1984

Can. J. Chem.

View full text Add to dashboard Cite

show abstract

“…It is clear from previous publications (17)(18)(19) that serum albumin has a variety of metal sites with different specificities, although the reported data are somewhat ambiguous. The best characterized metal sites on albumin are those for Cu 2ϩ and Ni 2ϩ , which bind strongly to a square-planar site of four nitrogen ligands from Asp-1-Ala-2-His-3 at the N terminus (20)(21)(22), and for Au ϩ (from antiarthritic drugs), which binds to the thiolate sulfur at Cys-34 (23).…”

mentioning

confidence: 99%

“…CD studies suggest that the major Zn 2ϩ site is also a secondary (weaker) binding site for Cu 2ϩ and Ni 2ϩ (17). Early 113 Cd NMR experiments on BSA demonstrated the existence of two Cd 2ϩ -binding sites (18), A and B. Competition experiments on bovine and HSAs (18,19,24) .…”

mentioning

confidence: 99%

Interdomain zinc site on human albumin

Stewart

Blindauer

Berezenko

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

170

183

View full text Add to dashboard Cite

Albumin is the major transport protein in blood for Zn 2؉ , a metal ion required for physiological processes and recruited by various drugs and toxins. However, the Zn 2؉ -binding site(s) on albumin is ill-defined. We have analyzed the 18 x-ray crystal structures of human albumin in the PDB and identified a potential five-coordinate Zn site at the interface of domains I and II consisting of N ligands from His-67 and His-247 and O ligands from Asn-99, Asp-249, and H 2O, which are the same amino acid ligands as those in the zinc enzymes calcineurin, endonucleotidase, and purple acid phosphatase. The site is preformed in unliganded apo-albumin and highly conserved in mammalian albumins. We have used 111 Cd NMR as a probe for Zn 2؉ binding to recombinant human albumin. We show that His-67 3 Ala (His67Ala) mutation strongly perturbs Cd 2؉ binding, whereas the mutations Cys34Ala, or His39Leu and Tyr84Phe (residues which may H-bond to Cys-34) have no effect. Weak Cl ؊ binding to the fifth coordination site of Cd 2؉ was demonstrated. Cd 2؉ binding was dramatically affected by high fatty acid loading of albumin. Analysis of the x-ray structures suggests that fatty acid binding to site 2 triggers a spring-lock mechanism, which disengages the upper (His-67͞Asn-99) and lower (His-247͞Asp-249) halves of the metal site. These findings provide a possible mechanism whereby fatty acids (and perhaps other small molecules) could influence the transport and delivery of zinc in blood.

show abstract

“…Indeed, it was reported that there exists chemical interactions between Cd(II), Zn(II), Ni(II), and Cu(II), and amino acid residues of albumin, such as histidine and aspartic acid. 12,17 The relatively small frequency shift for Ag(I) may result from its electric charge of +1 and a stable formation of the ammine complex in the buffer solution. Figure 5 indicates that the adsorption of Cd(II), Zn(II), Ni(II), and Co(II) became rapidly weak with increasing pH of more than pH 9.…”

Section: Denaturation Of Bsa Membrane and Adsorption Of Metal Ions Onmentioning

confidence: 99%

“…Indeed, it has been reported that Cd(II), Cu(II), Zn(II), and [PtCl4] 2-strongly interact with albumin. [12][13][14][15][16][17] Hence, it is assumed to be worthwhile to study the adsorption of metal ions onto a BSA membrane with a BSA-coated PQC for understanding the interaction between metal ions and BSA.…”

Section: Introductionmentioning

confidence: 99%

Adsorption Behavior of Metal Ions onto a Bovine Serum Albumin (BSA) Membrane Monitored by Means of an Electrode-Separated Piezoelectric Quartz Crystal

et al. 2005

View full text Add to dashboard Cite

Cadmium(II), zinc(II), and copper(II) ions binding to bovine serum albumin. A 113Cd NMR study

Cited by 55 publications

References 26 publications

The interactions of the chloride and bromide ions in nematic lyotropic liquid crystalline solution

The interactions of the chloride and bromide ions in nematic lyotropic liquid crystalline solution

Interdomain zinc site on human albumin

Adsorption Behavior of Metal Ions onto a Bovine Serum Albumin (BSA) Membrane Monitored by Means of an Electrode-Separated Piezoelectric Quartz Crystal

Contact Info

Product

Resources

About