Total synthesis of TASP 4a molecules by solid phase methods

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)]


Published in:
Innovation and perspectives in solid phase synthesis : peptides, polypeptides and oligonucleotides, macro-organic reagents and catalysts : collected papers, first international symposium, 39-50
Year:
1990
Laboratories:




 Record created 2006-02-09, last modified 2018-01-27


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