TY - JOUR
T1 - Supramolecular assembly of lysine-b-glycine block copolypeptides at different solution conditions
AU - Gaspard, Jeffery
AU - Silas, James A.
AU - Shantz, Daniel F.
AU - Jan, Jeng Shiung
N1 - Funding Information:
J.-S. Jan acknowledges start-up support from the National Cheng Kung University. J.-S. Jan and D.F. Shantz also acknowledge financial support from the Texas A&M University Life Science Task Force and Robert A. Welch Foundation (A-1638), J.M. Scholtz for access to the CD instrument, and the Chemistry Department at Texas A&M for access to the NMR facilities.
PY - 2010/3
Y1 - 2010/3
N2 - Here we report the supramolecular assembly of poly(l-lysine)-b-polyglycine diblock copolypeptides at different solution conditions. Light scattering and confocal microscopy indicate that the supramolecular aggregates initially formed in solution are vesicles with a broad size distribution, depending strongly on the initial processing conditions. The vesicles formed after multiple pH cycles appear independent of the initial processing conditions and are related to the thermodynamic nature of the assembled supramolecular aggregates. Circular dichroism results verify that this change in size observed over pH cyclings tracks with the conformation changes of the lysine block confined in the vesicle membranes. This appears interesting for peptosome-based materials, implying a high level of fluidity in the membrane that allows the supramolecular aggregates formed in solution to respond to changes in pH. The results also show that the external stimulus, which is the change of pH in this study, provides an additional means to regulate polypeptide vesicle size and size distribution.
AB - Here we report the supramolecular assembly of poly(l-lysine)-b-polyglycine diblock copolypeptides at different solution conditions. Light scattering and confocal microscopy indicate that the supramolecular aggregates initially formed in solution are vesicles with a broad size distribution, depending strongly on the initial processing conditions. The vesicles formed after multiple pH cycles appear independent of the initial processing conditions and are related to the thermodynamic nature of the assembled supramolecular aggregates. Circular dichroism results verify that this change in size observed over pH cyclings tracks with the conformation changes of the lysine block confined in the vesicle membranes. This appears interesting for peptosome-based materials, implying a high level of fluidity in the membrane that allows the supramolecular aggregates formed in solution to respond to changes in pH. The results also show that the external stimulus, which is the change of pH in this study, provides an additional means to regulate polypeptide vesicle size and size distribution.
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U2 - 10.1080/10610270903089746
DO - 10.1080/10610270903089746
M3 - Article
AN - SCOPUS:77951135515
SN - 1061-0278
VL - 22
SP - 178
EP - 185
JO - Supramolecular Chemistry
JF - Supramolecular Chemistry
IS - 3
ER -