Solution Structures of FcRI -Chain Mimics: A 
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- 作者：James M. McDonnell ; David Fushman ; Sean M. Cahill ; Brian J. Sutton ; and David Cowburn
- 刊名：Journal of the American Chemical Society
- 出版年：1997
- 出版时间：June 11, 1997
- 年：1997
- 卷：119
- 期：23
- 页码：5321 - 5328
- 全文大小：240K
- 年卷期：v.119,no.23(June 11, 1997)
- ISSN：1520-5126
文摘
A central event in the development of the allergic response is theinteraction between immunoglobulin E(IgE) and its cellular high-affinity receptor Fc
RI.Allergen-bound IgE mediates the allergic response bybindingthrough its Fc region to its cellular receptor on mast cells andbasophils, causing the release of chemical mediators. One strategy for the treatment of allergic disorders is theuse of therapeutic compounds which would inhibit the interaction between IgE and FcRI. Using astructure-based design approach, conformationally constrained synthetic peptides were designed to mimic a biologically active
-hairpin region of the 
-chain of FcRI.Two peptide mimics of the FcRI -chain were previously shownto inhibit IgE-FcRI interactions, one a peptidecomprised of L-amino acids, covalently cyclized by N- andC-terminal cysteine residues, and the other itsretroenantiomer. In this paper the solution structures of thesecompounds are derived using NMR spectroscopy.The topochemical relationship between the retroenantiomericcompounds and the structural basis of their biologicalactivity is described.
RI.Allergen-bound IgE mediates the allergic response bybindingthrough its Fc region to its cellular receptor on mast cells andbasophils, causing the release of chemical mediators. One strategy for the treatment of allergic disorders is theuse of therapeutic compounds which would inhibit the interaction between IgE and FcRI. Using astructure-based design approach, conformationally constrained synthetic peptides were designed to mimic a biologically active-hairpin region of the -chain of FcRI.Two peptide mimics of the FcRI -chain were previously shownto inhibit IgE-FcRI interactions, one a peptidecomprised of L-amino acids, covalently cyclized by N- andC-terminal cysteine residues, and the other itsretroenantiomer. In this paper the solution structures of thesecompounds are derived using NMR spectroscopy.The topochemical relationship between the retroenantiomericcompounds and the structural basis of their biologicalactivity is described.