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Ni(II) binding to 429-460 peptide fragment from human toll-like receptor (hTLR4)

Zoroddu, Maria Antonietta and Peana, Massimiliano Francesco and Medici, Serenella and Solinas, Costantino and Potocki, Sławomir and Kozlowski, Henryk (2013) Ni(II) binding to 429-460 peptide fragment from human toll-like receptor (hTLR4). In: 12. International symposium on metal ions in biology and medicine: abstracts and proceedings, March 11-13, 2013, Punta del Este, Uruguay. Montevideo, [s.n.]. p. 81. ISBN 978-9974-0-0911-0. Conference or Workshop Item.

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Abstract

Contact allergy, commonly induced by nickel, is the most frequent cause of contact hypersensitivity in industrialized countries, with 30% of population being affected. Ni(II) seems to trigger an inflammatory response by activating human Tool-like-Receptor 4 (hTLR4). Species-specific activation, as in this case, required distinct sequence motifs that are present in human but not in mouse, a species not sensitive to nickel-induced allergies. The specific region of human TLR4 responsible for nickel responses could be a sequence containing three histidine residues, H431, and the non- conserved H456 and H458, localized in the C-terminus. It has been proposed that the imidazole side chains of the histidine residues H456 and H458 provide a potential binding site for nickel because they were located at an optimal distance to interact with Ni(II) ions, whereas H431 was further apart. We decided to verify the possibility of metal binding to FQH431SNLKQMSEFSVFLSLRNLIYLDISH456TH458TR sequence, containing the three histidines supposedly involved in nickel response, in order to study the binding properties of the peptide fragment and on the thermodynamic stability of its metal complexes. Formation equilibria of Ni(II) complexes have been investigated in aqueous solution and in a wide pH range. Protonation and complex-formation constants have been potentiometrically determined; complex-formation models and species stoichiometry have been checked by means of UV-Vis absorption and CD spectroscopy and investigation through NMR is currently being carried out. The predominant species for a 1:1 peptide/Ni(II) molar ratio was obtained at physiological pH and showed an effective binding of the metal to the target sequence.

Item Type:Conference or Workshop Item (Poster)
ID Code:8872
Status:Published
Uncontrolled Keywords:Contact allergy, hTLR4, histidine residues
Subjects:Area 03 - Scienze chimiche > CHIM/03 Chimica generale e inorganica
Area 03 - Scienze chimiche > CHIM/01 Chimica analitica
Divisions:001 Università di Sassari > 01-a Nuovi Dipartimenti dal 2012 > Chimica e Farmacia
Publisher:[s.n.]
ISBN:978-9974-0-0911-0
Deposited On:22 Apr 2013 08:55

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