Protein design as a challenge for peptide chemists.
All efforts to turn the ultimate goal in protein de novo design into reality-the construction of new macromolecules with predetermined three-dimensional structure and well-defined functionality-failed because the mechanism of folding has still to be unravelled. In the present review, various attempts to apply synthetic tools for inducing native-like structural features in peptides in order to bypass the folding problem are described. Besides well-established methods for the nucleation and stabilization of secondary structures, e.g. alpha-helices, beta-sheets and beta-turns, topological templates as 'built-in' folding devices have more recently become the key elements for the induction of protein-like folding units (template-assembled synthetic proteins, TASP). Progress in the synthetic strategy and structural characterization of this new type of macromolecules opens the way for the design of functional TASP molecules.
Tuchscherer
G
G
Institute of Organic Chemistry, University of Lausanne, Switzerland.
Mutter
M
M
D001665:Binding Sites; D002384:Catalysis; D015195:Drug Design; D015394:Molecular Structure; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000138:chemical synthesis* / Q000737:chemistry
D011506:Proteins