Abstract

A report from a symposium on the recently developed strategy for protein de novo design, termed template-assembled synthetic proteins (TASPs), aimed to overcome the protein folding problem by constructing peptide sequences exhibiting nonlinear chain connectivities. In order to elucidate the potential of solid phase peptide synthesis for building up this new family of macromols., TASPs with the following structural features were designed: 1) a cyclic (1-10) template, Ac-Cys-Lys-Ala-Lys-Pro-Gly-Lys-Ala-Lys-Cys-NH2, and 2) four identical chains covalently bound to the e-amino function of the lysines. These chains were 11, 15, and 18 amino acids long as shown: Glu-Leu-Leu-|Glu-Ala-Leu-Glu-|Lys-Ala-Leu-Lys-Glu-Ala-Leu-Ala-Lys-Leu-Gly-. The peptides were assembled using a combination of tert-butoxycarbonyl (Boc) and 9-fluorenylmethoxycarbonyl (Fmoc) strategies on a methylbenzhydrylamine solid support. Conformational anal., using CD of the TASPs and individual chains, suggest a definite participation of the template in inducing and maintaining the predicted a-helical secondary structure of the 4-helix bundle. [on SciFinder (R)]

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