Immobilized replicates of sequence 136–148 of human serum albumin as adsorbents for bilirubin

Bouvier, Marlène; Brown, G. R.; St-Pierre, L. E.

doi:10.1139/v87-322

Cited by 12 publications

(9 citation statements)

References 16 publications

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“…Previous reports from this laboratory have demonstrated that certain peptides immobilized on a cross-linked polymer support form efficient adsorbents for bilirubin (6)(7)(8). This paper describes the adsorption behaviour of adsorbents with pendants synthesized from amino acids, such as lysine and arginine, that have been shown previously to be of key importance for the adsorption of bilirubin (6)(7)(8) and have been reported to be involved in the binding of bilirubin by HSA (9-1 1).…”

Section: Introductionmentioning

confidence: 95%

“…Peptide resins were hydrolyzed at 110°C for 48 h according to previously published procedures (8). Amino acid analyses were performed using a Varian 5500 Analyzer.…”

Section: Amino Acid Analysesmentioning

confidence: 99%

“…Studies in this laboratory have demonstrated that the presence of the basic amino acids, arginine and lysine, results in materials with a high binding capacity and strong affinity for bilirubin (7,8). Serine residues are incorporated into the sequence to provide the possibility of additional hydrogen bonding between the side-chain hydroxyl group and the hydrogen acceptor (two propionic acid groups and two lactam CO groups) or the hydrogen donor (four NH groups) on bilirubin.…”

Section: Rationalementioning

confidence: 99%

“…A normalization process, based on the results of the amino acid analyses, was applied to the experimental adsorption isotherms in a manner described previously (8). The normalized isotherms (Fig.…”

Section: Figmentioning

confidence: 99%

“…This paper describes the adsorption behaviour of adsorbents with pendants synthesized from amino acids, such as lysine and arginine, that have been shown previously to be of key importance for the adsorption of bilirubin (6)(7)(8) and have been reported to be involved in the binding of bilirubin by HSA (9-1 1). Residues of serine are also incorporated into the sequence.…”

Section: Introductionmentioning

confidence: 99%

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The binding of bilirubin by immobilized oligopeptides containing lysine

Bouvier¹,

Brown²,

St-Pierre³

1989

Can. J. Chem.

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. Can. J. Chem. 67, 596 (1989).Peptides consisting of portions of the sequence Arg-(Ly~)~-(Ser)~-Lys-(Ala)~ have been immobilized onto a polyacrylamide support by solid phase peptide synthesis. Isotherms at 0°C for the adsorption of bilirubin from phosphate buffer by these peptide resins are highly dependent on pH, in the range 7.80-11.00, demonstrating the importance of ionic interactions. The adsorption behaviour of bilirubin-related tetrapyrroles shows that structural factors also influence the process. Peptide resins containing two or more residues of lysine have two binding sites on each pendant and are characterized by positive cooperativity , to a degree that is highly dependent on the number of residues. It is proposed that bilirubin molecules bound by lysine-containing pendants are stacked, the dimer state being stabilized by T-w electron interactions, hydrogen bonds, and hydrophobic interactions. Site binding constants show that arginine-containing pendants manifest a stronger affinity for bilirubin.Key words: bilirubin, adsorption, lysine, oligopeptides, cooperativity. Chem. 67,596 (1989).Des peptides consistant en diffkrentes portions de la sCquence Arg-(Ly~)~-(Ser)~-Lys-(Ala)~ ont Ct C greffCs, via la technique de synthkse en phase solide des peptides, i un support de polyacrylamide rCticulC. Des isothermes caracterisant I'adsorption de la bilirubine en milieu tampon, B O°C, par ces adsorbants sont dCpendants du pH, dans l'inte~alle 7,80-11,00, dCmontrant ainsi l'importance des interactions ioniques. L'adsorption de tCtrapyrroles similaires B la molCcule de bilirubine a dCmontrC que des facteurs reliCs i la structure du ligand influencent 1e processus d'association. Les adsorbants qui contiennent deux rksidus de lysine ou plus ont deux sites d'adsorption par pendant et sont caractCrisCs par un mode d'adsorption B coopCrativitC positive, le degrC duquel est dependant du nombre de residus de lysine dans la sCquence. I1 est propose que les pendants contenant des rksidus de lysine favorisent la dimtrisation des molCcules de bilirubine liCes, le dimere Ctant stabilisC par des interactions w-a, des ponts hydrogenes et des interactions hydrophobiques. Des constantes d'association ont dCmontrCes que les pendants qui contiennent des rCsidus d'arginine manifestent une grande affinitC pour la bilirubine.

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Section: Introductionmentioning

confidence: 95%

“…Peptide resins were hydrolyzed at 110°C for 48 h according to previously published procedures (8). Amino acid analyses were performed using a Varian 5500 Analyzer.…”

Section: Amino Acid Analysesmentioning

confidence: 99%

Section: Rationalementioning

confidence: 99%

Section: Figmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

The binding of bilirubin by immobilized oligopeptides containing lysine

Bouvier¹,

Brown²,

St-Pierre³

1989

Can. J. Chem.

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The influence of charge density and steric factor of aminated chloromethyl polystyrene homologs in bilirubin adsorption

Raghavan

Shaligram

Deshpande

1991

J of Applied Polymer Sci

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SYNOPSISBilirubin, a bile pigment, was studied for its extent of adsorption on substituted aminechloromethyl polystyrene by UV spectrophotometry. By performing simple displacement reactions on chloromethyl polystyrene with secondary and tertiary amines, the amount of charge density and steric factor on substituted nitrogen atom have been varied. Adsorption isotherms of bilirubin at 0°C by different amine-chloromethyl polystyrene homologs suggest the existence of electrostatic interaction of polymeric resin with bilirubin moiety. Results of adsorption of bilirubin to polymeric resin have shown that the extent of adsorption of bilirubin depends on the unit charge, and on the structure of the substituted amine-chloromethyl polystyrene. The effects of porosity of resin on bilirubin adsorption have also been discussed.

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A simplified analysis of scatchard plots for systems with two interacting binding sites

et al. 1988

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SynopsisA simple graphical method for calculating stoichiometric and site binding constants for systems with two initially equivalent interacting sites is derived from a modified Scatchard equation. The binding constants can be calculated from Scatchard plots ( r / [ A ] as a function of r ) using the values of r / [ A ] ( r is the molar ratio of bound ligands to total protein and [ A ] is the equilibrium concentration of free ligand) when r = 0 and r = 1 (half-saturation). The applicability of the method to the adsorption of bilirubin by peptide pendants immobilized on a polyacrylamide support is demonstrated.

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Immobilized replicates of sequence 136–148 of human serum albumin as adsorbents for bilirubin

Cited by 12 publications

References 16 publications

The binding of bilirubin by immobilized oligopeptides containing lysine

The binding of bilirubin by immobilized oligopeptides containing lysine

The influence of charge density and steric factor of aminated chloromethyl polystyrene homologs in bilirubin adsorption

A simplified analysis of scatchard plots for systems with two interacting binding sites

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