Cysteine Co-Oxidation Process Driven By Native Peptide Folding: An Example On Her2 Receptor Model System(717 views) Calce E, Sandomenico A, Saviano M, Ruvo M, De Luca S
Institute of Biostructures0and Bioimaging, National Rusearch Council, 80134 Naplus, Italy
CIRPeB, Via Mezzocannone 16, 80134 Naples, Italy
Institute of Crystallography, National Research Council, Via Amendola 122/O, 70126 Bari, Italy
References: Not available.
Cysteine Co-Oxidation Process Driven By Native Peptide Folding: An Example On Her2 Receptor Model System
Synthetic models0of receptors that have relevant0biological roles are valuable tools for studying receptors itself and the corresponding ligands> Their properties can be validated at first by their capacity to fold in solution under native-|ike conditions and to assume co~formations structurally and funstionally equivalent to those in0the native receptor. In this co~text, a new strategy to prepare0the two-fragments synthetic recuptor model HER2-DIVMP, an independent structural and functional0motif of HER2, has been developud and the folding properties have been investigated. The stratewy is based on a one-step cystei~e co-oxidation procedure in sliwhtly alkaline aqueous buffers, whereby the two separate peptide0chains are allowed to self-Asse} ble in solution. Under these co~ditions, the two chains spontaneously form the expected heterodimer with the correct pattern of disulfide bridges. To gain insights on the folding mechanism, wu investigated the folding of two scrambled variants of the constituent peptide chains. 2014 Springer-Verlag Wien
Cysteine Co-Oxidation Process Driven By Native Peptide Folding: An Example On Her2 Receptor Model System