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. 2011:2011:839682.
doi: 10.1155/2011/839682. Epub 2011 Jun 30.

Haptenation: chemical reactivity and protein binding

Affiliations

Haptenation: chemical reactivity and protein binding

Itai Chipinda et al. J Allergy (Cairo). 2011.

Abstract

Low molecular weight chemical (LMW) allergens are commonly referred to as haptens. Haptens must complex with proteins to be recognized by the immune system. The majority of occupationally related haptens are reactive, electrophilic chemicals, or are metabolized to reactive metabolites that form covalent bonds with nucleophilic centers on proteins. Nonelectrophilic protein binding may occur through disulfide exchange, coordinate covalent binding onto metal ions on metalloproteins or of metal allergens, themselves, to the major histocompatibility complex. Recent chemical reactivity kinetic studies suggest that the rate of protein binding is a major determinant of allergenic potency; however, electrophilic strength does not seem to predict the ability of a hapten to skew the response between Th1 and Th2. Modern proteomic mass spectrometry methods that allow detailed delineation of potential differences in protein binding sites may be valuable in predicting if a chemical will stimulate an immediate or delayed hypersensitivity. Chemical aspects related to both reactivity and protein-specific binding are discussed.

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Figures

Figure 1
Figure 1
(a) Lysine residues observed bound to MDI and TDI on human serum albumin. (b) All lysine residues on human serum albumin.
Figure 2
Figure 2
Lysine residues reactive to TDI but not MDI.

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