Antiparallel 3-Sheet Based Nanofibers

Schneider and Pochan (2002) have described a different system of peptides with alternating polar and hydrophobic residues composed of Val as an amino acid with high -sheet forming propensity and Lys as a modulator of pH-dependent self-assembly. Self-assembly was designed to be triggered by intramolecular folding into a /3-hairpin structure based on the stereochemistry of central Pro residues (Fig. 14.8). 

Systematic smdies were carried out to understand the mechanism of molecular self-assembly into a macroscopic hydrogel structure by a variety of biophysical 

Gontrolled nanostructural morphology, in this case nanofibers with controlled length, was achieved by varying the ratio of the central repeating number of (Gin-Leu) and the flanking lysine residues. A variety of biophysical characterization methods indicated that the short, dispersed nanofibers formed by K2(QL)gK2 reached 

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