Hydrophobic interactions, self-assembled molecules peptides

Figure 4.2 Self-assembling peptide amphiphiles (PA) used for biomimetic mineralization of HA/PA nanocomposite, (a) Chemical structure of the PA, comprising 5 regions (1) a hydrophobic alkyl tail (2) four cysteine residues that can form disulfide bonds to polymerize the self-assembled structure (3) a flexible linker region of three glycine residues (4) a single phosphorylated serine residue that was able to interact strongly with calcium ions and help direct mineralization of HA (5) the cell adhesion ligand ROD. (b) Molecular model of one single PA molecule, (c) Schematic showing the self-assembly of PA molecules into a cylindrical micelle.

Figure 6.3 Self-assembled nanostructures based on P-sheet (a) peptides packing into sheets and fibers based on hydrophobic interactions on one face of the molecule, and complementary ionic interaction on the other (b) peptides with alternating hydrophilic and hydrophobic residues assemble into P-sheet structures (left) that form twisted ribbons (right) and bundle into larger fibers and (c) self-assembly based on amphiphilic triblock peptides, where the central hydrophobic block forces self-assembly via hydrophobic interactions between molecules and hydrogen bonding along the fiber axis.

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