Template-assembled synthetic protein conformation

Fig. 4. Schematic representation of template-assembled synthetic proteins. The conforma-tionally restricted template can be orthogonally protected and sequentially linked to helical segments to form a large variety of functionalized TASP proteins. Flexible spacers that connect the folded peptide segments and the template provide the necessary conformational freedom that will allow the hydrophobic residues to find their optimum orientations for packing the core...

Mutter M, Tuchscherver GG, Miller GG, Altmann K-H, Carey RI, Wyss DF, Labhard AM, Rivier JE. Template-assembled synthetic proteins with four-helix-bundle topology. Total chemical synthesis and conformational studies. J Am Chem Soc 1992 114 1463-1470. 

Leufgen et al. [82] reported the investigation of a template-assembled synthetic protein (TASP) conformation and its orientation in self-assembled monolayers (SAM) by means of TOF-SIMS. In this study, both the presence and molecular orientation of the TASP molecule can be monitored by TOF-SIMS, and furthermore, the influence of self-assembly protocols on the TASP molecular surface orientation can be studied by TOF-SIMS, although Fourier transform infrared spectroscopy (FTIR) and surface plasmon resonance (SPR) fail in this case. 

As with the three polymeric examples, bipyridine ligands have been incorporated into polypeptides at the chain end, in the backbone, and as attached substituents. Specifically, a bipyridine has been coupled to either the amino or acid terminus of polypeptides to afford biological macroligands. For example, the 4,4 -dicarboxylic acid bipyridine was coupled to two 14-unit o-helices in order to analyze the conformation of the parallel structures.272 A triple-helical synthetic metallo-protein was formed through metal-templated self-assembly of a bipyridine unit with a 15-residue peptide substituted in the presence of metal ions.273... 

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