An FcgammaRIIa-binding peptide that mimics the interaction between FcgammaRIIa and IgG.

An FcgammaRIIa-binding peptide that mimics the interaction between FcgammaRIIa and IgG. Research Abstract Details 

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An FcgammaRIIa-binding peptide that mimics the interaction between FcgammaRIIa and IgG. Abstract Text:

Angela C Cendron,Bruce D Wines,Robert T C Brownlee,Paul A Ramsland,Geoffrey A Pietersz,P Mark Hogarth,

A disulphide-constrained peptide that binds to the low affinity Fc receptor, FcgammaRIIa (CD32) has been identified and its structure solved by NMR. Linear (7-mer and 12-mer) and disulphide-constrained (7-mer) phage display peptide libraries were panned on recombinant soluble FcgammaRIIa genetically fused to HSA (HSA-FcgammaRIIa). Peptides were isolated only from the constrained peptide library and these contained the consensus sequence, CWPGWxxC. Phage clones displaying variants of the peptide consensus sequence bound to FcgammaRIIa and the strongest binding clone C7C1 (CWPGWDLNC) competed with IgG for binding to FcgammaRIIa and was inhibited from binding to FcgammaRIIa by the FcgammaRIIa-blocking antibody, IV.3, suggesting that C7C1 and IgG share related binding sites on FcgammaRIIa. A synthetic disulphide-constrained peptide, pep-C7C1 bound to FcgammaRIIa by biosensor analysis, albeit with low affinity (KD approximately 100microM). It was significant that the FcgammaRIIa consensus peptide sequence contained a Proline (Pro3), which when substituted with alanine abrogated FcgammaRIIa binding, consistent with Pro3 contributing to receptor binding. Upon binding of IgG and IgE to their respective Fc receptors (FcgammaRs and FcepsilonRI) Pro329 in the Fc makes a critical interaction with two highly conserved Trp residues (Trp90 and Trp113) of the FcRs. The NMR structure of pep-C7C1 revealed a stabilizing type II beta-turn between Trp2 and Trp5, with Pro3 solvent exposed. Modelling of the pep-C7C1 structure in complex with FcgammaRIIa suggests that Pro3 of C7C1 binds to FcgammaRIIa by inserting between Trp90 and Trp113 of FcgammaRIIa thereby mimicking the molecular interaction made between FcgammaRIIa and IgG.

An FcgammaRIIa-binding peptide that mimics the interaction between FcgammaRIIa and IgG. Publishing Authors By Initials

AC Cendron,BD Wines,RT Brownlee,PA Ramsland,GA Pietersz,PM Hogarth,

For similar natural sciences: chemistry: chemistry, physical: surface properties research abstracts see: natural sciences: chemistry: chemistry, physical: surface properties research

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An FcgammaRIIa-binding peptide that mimics the interaction between FcgammaRIIa and IgG. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Molecular immunology

VOLUME: 45

Page Numbers: 307-19

Journal Abbreviation: Mol. Immunol.

ISSN: 0161-5890

DAY: 30

MONTH: 07

YEAR: 2007

An FcgammaRIIa-binding peptide that mimics the interaction between FcgammaRIIa and IgG. Information

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LANGUAGE: eng

NlmUniqueID: 7905289

An FcgammaRIIa-binding peptide that mimics the interaction between FcgammaRIIa and IgG. Keywords Mesh Terms:

KEYWORDS: Surface Properties

MESH TERMS: metabolism

Chemical & Substance for Abstract: An FcgammaRIIa-binding peptide that mimics the interaction between FcgammaRIIa and IgG. Information

Substance Name: Serum Albumin

Registry Number: 0

Grant and Affiliation Information for An FcgammaRIIa-binding peptide that mimics the interaction between FcgammaRIIa and IgG.

AFFILIATION: Burnet Institute, Austin Campus, Studley Road, Heidelberg, Vic. 3084, Australia.

Country: England

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MEDLINETA: Mol Immunol

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