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Finding Using Conformationally Constrained Peptides Mimicking Exposed Protein Epitopes

Lead Finding Using Conformationally Constrained Peptides Mimicking Exposed Protein Epitopes [Pg.5]

Type-1 IFNR Type-ll IFNRu Type-ll IFNRp IL-10 [Pg.8]

Type-1 TNFR Type-ll TNFH NGFR Fas CD40 [Pg.8]

Structural data is also available for tumor necrosis factor (TNF) bound to a soluble fragment of its receptor37 in a 3 1 receptonligand stoichiometry, and for tissue factor [Pg.10]

Several potent inhibitors of fibrinogen binding to gpIIb/IIIa are now known, and some have proven to be effective antithrombotic agents. These inhibitors tend either to be small cyclic peptide mimetics, in which the conformation of an RGD sequence is constrained by macrocyclization, or they are non-peptidic molecules containing functional group mimetics of the Arg and Asp side chains, held in the correct geometry for interaction with the receptor. Examples of both classes are shown in [Pg.14]




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Conformational epitope

Conformational peptides

Conformational protein

Conformationally constrained

Epitope

Exposive

Mimicking

Peptide conformation

Peptides conformationally constrained

Protein using

Proteins conformation

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