Triple helix peptide

Kar K, Amin P, Bryan MA, Persikov AV, Mohs A, Wang Y-H, Brodsky B. Self-association of collagen triple helix peptides into higher order structures. J Biol Chem 2006 281 33283-33290. 

Fig. 7. Structure of the integrin I domain bound to the IBP triple-helix peptide.

Genetically Modified Collagen-like Triple Helix Peptide as Biomimetic Template... 

GENETICALLY MODIFIED COLLAGEN-LIKE TRIPLE HELIX PEPTIDE... 

Triple helix peptide nanowires of interest for material applications are based on the motif of type I collagen. In type I collagen, the triple helix molecule is a heterotrimer comprised of two identical al chains and one a2 chain. The al and a2 chains are very similar with over 95% identity on amino acid sequence. Each a-chain contains over 1000 amino acids and has a molecular weight of approximately 95,000 Da. These molecules of type I collagen have a length of slightly less than 300 nm and diameter of about 1.4nm (Figure 9.2)." ... 

CONFORMATION OF TRIPLE HELIX PEPTIDES FROM COLLAGEN... 

The stability of triple helix peptide is especially important for material applications because wild-type collagens are not stable enough to be ineorporated as building blocks that could be used in a harsh environment. Their meehanieal property also needs to be enhanced to develop metal and semiconductor coatings so that they are stable enough to resist under extreme chemical conditions. To develop a strategy to improve the stability, we first need to understand how chemical interactions between these peptides nucleate and assemble collagen triple helix peptides. 

The presence of foldon and Cys knot is the key to nucleate the triple helix peptide. The C-terminal domain of T4 fibritin (foldon) is obligatory for the formation of the fibritin trimer structure and can be used as an artificial trimerization domain. The C-terminal part of the T4 fibritin trimer is formed from the trimeric coiled-coil domain, which is terminated by a C-terminal trimeric [3-sheet propeller consisting of... 

Figure 9.3. (a) Construction of a recombinant protein fragment that models 63 amino acids sequence, residues 877-939, of type I collagen, (b) TEM image of these triple helix peptide nanowires is shown in the bottom right. 

In the previous section, we introduced a genetically modified coUagen-Uke triple helix peptide F877 by recombinant technology as a rigid and monodispersed... 

In this section, we introduce another example of this triple helix peptide coating with oxide semiconductors. This biotemplating method can address both needs for... 

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