TY - JOUR
T1 - Spontaneous vesicle formation by helical glycopeptides in water
AU - Kimura, Shunsaku
AU - Muraji, Yuichi
AU - Sugiyama, Junji
AU - Fujita, Katsuhiko
AU - Imanishi, Yukio
N1 - Funding Information:
We thank Professor K. Kaji and Dr. T. Kanaya for the DLS measurements. This work is partly supported by Iketani Science and Technology Foundation, Japan.
PY - 2000/2/15
Y1 - 2000/2/15
N2 - Hydrophobic helical peptide molecules with a lactose unit at the C terminal, Nap-(Ala-Aib)(n)-NHCH 2 CH 2 NH-Lac (Nap, Aib, and Lac represent 2- naphthylacetic acid group, 2-aminoisobutyric acid, and lactobionic acid group, respectively, n = 4, 6, 8), were synthesized and their formation of self-assemblies in water was investigated. Nap-(Ala-Aib) 4 -NHCH 2 CH 2 NH-Lac was spontaneously dispersed in water and formed aggregates of 70 nm diameter, shown by dynamic light scattering measurement. Cryo-TEM observation revealed that the aggregates took on a vesicular structure with a single membrane. The membrane is suggested to be composed of helical peptide molecules with an interdigitated antiparallel packing on the basis of circular dichroism and fluorescence measurements. On the other hand, the dodecapeptide formed a fibrous assembly, and the hexadecapeptide could not be dispersed in water. (C) 2000 Academic Press.
AB - Hydrophobic helical peptide molecules with a lactose unit at the C terminal, Nap-(Ala-Aib)(n)-NHCH 2 CH 2 NH-Lac (Nap, Aib, and Lac represent 2- naphthylacetic acid group, 2-aminoisobutyric acid, and lactobionic acid group, respectively, n = 4, 6, 8), were synthesized and their formation of self-assemblies in water was investigated. Nap-(Ala-Aib) 4 -NHCH 2 CH 2 NH-Lac was spontaneously dispersed in water and formed aggregates of 70 nm diameter, shown by dynamic light scattering measurement. Cryo-TEM observation revealed that the aggregates took on a vesicular structure with a single membrane. The membrane is suggested to be composed of helical peptide molecules with an interdigitated antiparallel packing on the basis of circular dichroism and fluorescence measurements. On the other hand, the dodecapeptide formed a fibrous assembly, and the hexadecapeptide could not be dispersed in water. (C) 2000 Academic Press.
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U2 - 10.1006/jcis.1999.6643
DO - 10.1006/jcis.1999.6643
M3 - Editorial
AN - SCOPUS:0034652414
SN - 0021-9797
VL - 222
SP - 265
EP - 267
JO - Journal of Colloid And Interface Science
JF - Journal of Colloid And Interface Science
IS - 2
ER -