Part of the Advances in Experimental Medicine and Biology book series (volume 611)
Peptides binding the type E immunoglobulins
The human high affinity IgE receptor, hFcεRI, found on the surface of mast cells and basophils, is believed to mediate allergic diseases, anaphylaxis and asthma through binding of IgE itself. hFcεRI contains four distinct polypeptide chains: an α chain, a β chain and a dimer of γ chains. The extracellular portion of the α chain binds with high affinity to the Fc region of the IgE (K D=10 −9M), whereas the β and γ chains are responsible for down-stream signal propagation through phosphorylation of their intracytoplasmatic immunoreceptor tyrosine-based activation motifs (ITAM) [ 1]. In the effort to obtain a receptor antagonist working by binding the soluble IgE, we have designed a peptide-based receptor mimetic on the basis of the crystallographic structure of the complex between the hFceRI α chain and the IgE Fc portion [ 2]. To this aim, fragments containing key residues for Fcε interaction and derived from the D2 domain (interaction site 1, Y129–H134, [ 2]) and D1–D2...
KeywordsSensor Chip Binding Curf Spontaneous Oxidation Modest Influence Synthetic Construct
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Financial support from project FIRB RBNE03PX83_005 is acknowledged.
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