Protein design as a challenge for peptide chemists

✍ Scribed by Gabriele Tuchscherer; Manfred Mutter

• Publisher: John Wiley and Sons
• Year: 1995
• Tongue: English
• Weight: 641 KB
• Volume: 1
• Category: Article
• ISSN: 1075-2617
• DOI: 10.1002/psc.310010103

✦ Synopsis

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.