Binding of Histamine and Antihistamine to Bovine Serum Albumin by Mediation with Cu(II)

Andrews, A. C.; Lyons, T. D.

doi:10.1126/science.126.3273.561

Cited by 7 publications

(3 citation statements)

References 3 publications

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“…3b,c ). This progressive loss of histamine binding may be because of its degradation by histaminases present in the incubation medium 23 24 , or to its unspecific binding to heparin on cell membrane 32 or to bovine serum albumin (BSA) 33 . As we have shown that our compounds could internalize CXCR4, we studied the effect of CXCR4 natural ligand, CXCL12, on pDC activation.…”

Section: Resultsmentioning

confidence: 99%

Natural amines inhibit activation of human plasmacytoid dendritic cells through CXCR4 engagement

et al. 2017

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Plasmacytoid dendritic cells (pDC) are specialized in secretion of type I interferon in response to pathogens. Here we show that natural monoamines and synthetic amines inhibit pDC activation by RNA viruses. Furthermore, a synthetic analogue of histamine reduces type I interferon production in a mouse model of influenza infection. We identify CXC chemokine receptor 4 (CXCR4) as a receptor used by amines to inhibit pDC. Our study establishes a functional link between natural amines and the innate immune system and identifies CXCR4 as a potential ‘on-off' switch of pDC activity with therapeutic potential.

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Section: Resultsmentioning

confidence: 99%

Natural amines inhibit activation of human plasmacytoid dendritic cells through CXCR4 engagement

et al. 2017

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“…L'histamine forme avec certains m6taux de transition des compos6s de coordination dont quelques propri6t6s physiologiques, pharmacologiques et biologiques importantes ont 6t6 mises en 6vidence par Gurd & Wilcox (1956), Andrews & Lyons (1957), Andrews, Lyons & O'Brien (1962) et Andrews & Romary (1964). En particulier, l'affinit6 sp6ciale que l'histamine des neurones, l'un des facteurs de r6gulation de la croissance cellulaire, pr6sente pour les m6taux canc6rig~nes, est signal6e par Hatem (1958Hatem ( ,1960.…”

Section: Introductionunclassified

Etude cristallographique du perchlorate de dihistamino-cuivre(II)

Bonnet¹,

Jeannin²

1970

Acta Crystallogr Sect B

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(Refu le 10 mars 1969) Dihistaminocopper(II) perchlorate, Cu(C6HsN3)2(C104)2, crystallizes in the monoclinic system: a= 8.235 + 0-006, b = 13.676 + 0-009, c= 8.084 + 0.006 A, p= 100 ° 5' + 5' and Z= 2; space group P21/c. 1099 independent (hkl) reflexions of a single crystal, shaped like a truncated pyramid, have been measured at room temperature. Convergent refinement by the full-matrix least-squares method, with anisotropic temperature factors, led to a weighted R index of 9"4% including zero reflexions. Two histamine molecules are chelated to one copper atom, each one being bound by two nitrogen atoms, one -N(1)-belonging to the imidazole ring and one -N(3)H2 belonging to the side chain. Perchlorate ions build chains parallel to the a axis; they are 'semi-coordinated' to the copper atom of a complex ion

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“…As far as we know, no study has investigated the relationship between BSA and histamine. Only a relatively old study reported the interaction of Cu(II)-BSA complex with histamine [24]. In our study, the binding affinity of BSA and histamine in physiologically relevant conditions was investigated using the CE-FA technique for the first time.…”

Section: Introductionmentioning

confidence: 98%

The affinity of histamine to serum albumin: Capillary electrophoresis‐frontal analysis and in‐silico molecular docking approaches

Kalaycıoğlu

2023

J of Separation Science

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Histamine is a biogenic amine found in various body tissues and responsible for many critical vital activities. It is also responsible for allergic reactions in the body. Ingestion of foods containing high amounts of histamine can cause fatal allergic reactions. Albumin in plasma controls drugs and free concentrations of bioactive constituents taken to the body with food. Hence, this study aimed to characterise the interactions of histamine with bovine serum albumin. Capillary electrophoresis in the frontal analysis mode was employed in this study as a practical approach for assessing histamine‐bovine serum albumin affinity. The plateau‐shaped free histamine peak was well separated from the bovine serum albumin (BSA)‐histamine complex peak. The free histamine concentration was obtained by following the height of the free histamine peak. Whereas the bound histamine concentrations were obtained by calculating the difference between the height of total and free histamine peaks. Histamine bound to BSA at one independent site with a Kb value of 2.50 × 103 L/mol. Moreover, an in‐silico molecular docking method was performed, and it was revealed that the binding site of histamine was located closer to Lysine‐131 in subdomain IIA of bovine serum albumin.

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Binding of Histamine and Antihistamine to Bovine Serum Albumin by Mediation with Cu(II)

Cited by 7 publications

References 3 publications

Natural amines inhibit activation of human plasmacytoid dendritic cells through CXCR4 engagement

Natural amines inhibit activation of human plasmacytoid dendritic cells through CXCR4 engagement

Etude cristallographique du perchlorate de dihistamino-cuivre(II)

The affinity of histamine to serum albumin: Capillary electrophoresis‐frontal analysis and in‐silico molecular docking approaches

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