The coordination properties of a small peptide fragment from Human TLR4 sequence are relevant in Nickel Allergy mechanism
Abstract
Data di Pubblicazione:
2016
Citazione:
The coordination properties of a small peptide fragment from Human TLR4 sequence are relevant in Nickel Allergy mechanism / Alessio, Pelucelli; Peana, Massimiliano Francesco; Giancarlo, Simula; Medici, Serenella; Solinas, Costantino; Zoroddu, Maria Antonietta. - (2016), pp. 11-11. (Intervento presentato al convegno XIV edizione del convegno La Parola ai Giovani 2016 tenutosi a Complesso Didattico – Via Vienna 2 – Sassari nel 28 Ottobre 2016).
Abstract:
Nickel Allergy (NA) is a contact allergy which could occur in sensitised persons exposed
for long periods of time to objects containing Nickel. In recent years, the human TLR4
(hTLR4) has been recognized as a key target in the Nickel-induced inflammation that
eventually lead to allergy symptoms [1]. A peptide of 32 amino acids from 429-460
sequence of hTLR4 receptor has been selected as a simplified model to study the
molecular mechanism of NA. The fragment contains three histidines, the non-conserved
H431, and the conserved H456 and H458 in human (Fig. 1) which could be important for
Ni(II) activation hTLR4 and to trigger an inflammatory response. The aim of our study
was to confirm the coordination ability of a peptide fragment toward the H456 and H458
histidines potentially involved in hTLR4 activation. Spectroscopic (NMR, UV-Vis, CD,
MS) and potentiometric techniques confirm the important role of the histidine-rich 429-
460 hTLR4 fragment in Ni(II) coordination and its relevance in NA mechanism [2].
for long periods of time to objects containing Nickel. In recent years, the human TLR4
(hTLR4) has been recognized as a key target in the Nickel-induced inflammation that
eventually lead to allergy symptoms [1]. A peptide of 32 amino acids from 429-460
sequence of hTLR4 receptor has been selected as a simplified model to study the
molecular mechanism of NA. The fragment contains three histidines, the non-conserved
H431, and the conserved H456 and H458 in human (Fig. 1) which could be important for
Ni(II) activation hTLR4 and to trigger an inflammatory response. The aim of our study
was to confirm the coordination ability of a peptide fragment toward the H456 and H458
histidines potentially involved in hTLR4 activation. Spectroscopic (NMR, UV-Vis, CD,
MS) and potentiometric techniques confirm the important role of the histidine-rich 429-
460 hTLR4 fragment in Ni(II) coordination and its relevance in NA mechanism [2].
Tipologia CRIS:
4.2 Abstract in Atti di convegno
Elenco autori:
Alessio, Pelucelli; Peana, Massimiliano Francesco; Giancarlo, Simula; Medici, Serenella; Solinas, Costantino; Zoroddu, Maria Antonietta
Link alla scheda completa:
Titolo del libro:
La Parola ai Giovani 2016