TY - JOUR
T1 - Supramolecular systems composed of α-helical peptides
AU - Imanishi, Yukio
AU - Fujita, Katsuhiko
AU - Miura, Yoshiko
AU - Kimura, Shunsaku
N1 - Funding Information:
monolayer. This interpretation is supported by fluorescencem icroscope observation of the peptide monolayer. The domain formation of the monolayer containing a fluorescence-labellehde lix was observed under a fluorescencem icroscopew hen the compression was held at the mound12.I n addition, fluorescence anisotropy was observed. These observations support the phase transition from a liquid to a solid state (two-dimensional crystal) around the mound region. n-A isotherm of Boc-(Leu-Aib)s-OBzl showed a steeps lope,i ndicatingf ormation of peptidem onolayer in a solid state.C omparison of the moleculara rea at the inflection point with the sectional area of the peptideb y molecularm odellings uggeststh at the side chainso f Leu residueo f a helix penetratein to a groove of the other helix, so that an interdigitation state appears. The molecular packing of Boc-(Leu-Aib)s-OBzl should be so tight due to interdigitationt hat a solid monolayeri s formed. n-A isotherm of Boc-(Lys(Z)-Aib)s-OMe showed a gentle slope with a relatively low collapse pressure, indicating the monolayer in a liquid state. The side chainso f Lys(Z) residuel ie on the surfaceo f the helix rod without interdigitation.T he bulky side chains of Lys(Z) residue might sterically hinder the molecular packing,r esultingi n a liquid monolayer.
PY - 1996
Y1 - 1996
N2 - Hydrophobic helical peptides having alternating hydrophobic amino acid and Aib in the sequence were synthesized to construct supramolecular systems. Three types of supramolecular systems were constructed by the peptides and the derivatives in different environments. First, the dispersion of TFA·H-(Ala-Aib)8-OBzl in water was studied by dynamic light scattering, which suggests the formation of a vesicular structure with an average diameter of 76 nm. We call the peptide assembly in water `peptosome'. Second, Boc-Ser(Ant)-(Ala-Aib)8-OMe spanned the phospholipid bilayer membrane and formed a helix-bundle structure. The bundle structure was supported by ion-channel formation in the membrane. Third, Boc-(Ala-Aib)8-OMe and Boc-(Leu-Aib)8-OBzl formed a two-dimensional crystal at the air-water interface. Boc-(Ala-Aib)12-OBzl also formed a monolayer in a solid state at the air-water interface, but the helix orientation was perpendicular to the interface, which presents a contrast to the parallel orientation of the former hexadecapeptides.
AB - Hydrophobic helical peptides having alternating hydrophobic amino acid and Aib in the sequence were synthesized to construct supramolecular systems. Three types of supramolecular systems were constructed by the peptides and the derivatives in different environments. First, the dispersion of TFA·H-(Ala-Aib)8-OBzl in water was studied by dynamic light scattering, which suggests the formation of a vesicular structure with an average diameter of 76 nm. We call the peptide assembly in water `peptosome'. Second, Boc-Ser(Ant)-(Ala-Aib)8-OMe spanned the phospholipid bilayer membrane and formed a helix-bundle structure. The bundle structure was supported by ion-channel formation in the membrane. Third, Boc-(Ala-Aib)8-OMe and Boc-(Leu-Aib)8-OBzl formed a two-dimensional crystal at the air-water interface. Boc-(Ala-Aib)12-OBzl also formed a monolayer in a solid state at the air-water interface, but the helix orientation was perpendicular to the interface, which presents a contrast to the parallel orientation of the former hexadecapeptides.
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U2 - 10.1016/0968-5677(96)00014-4
DO - 10.1016/0968-5677(96)00014-4
M3 - Article
AN - SCOPUS:0030103932
SN - 0968-5677
VL - 3
SP - 13
EP - 18
JO - Supramolecular Science
JF - Supramolecular Science
IS - 1-3
ER -