Molecular self-assembly of surfactant-like peptides to form nanotubes and nanovesicles.

Several surfactant-like peptides undergo self-assembly to form nanotubes and nanovesicles having an average diameter of 30-50 nm with a helical twist. The peptide monomer contains 7-8 residues and has a hydrophilic head composed of aspartic acid and a tail of hydrophobic amino acids such as alanine, valine, or leucine. The length of each peptide is approximately equal to 2 nm, similar to that of biological phospholipids.

Water Exchange and Rotational Dynamics of the Dimeric Gadolinium(III) Complex [BO{Gd(DO3A)(H(2)O)}(2)]: A Variable-Temperature and -Pressure (17)O NMR Study(1).

Rapid water exchange and slow rotation are essential for high relaxivity MRI contrast agents. A variable-temperature and -pressure (17)O NMR study at 14.1, 9.