pH responsiveness of block copolymer vesicles with a polypeptide corona.
The aggregation behavior of polybutadiene165-block-poly(L-lysine)88 in saline solution was studied by combined static and dynamic light scattering analyses. Vesicles were observed if the polypeptide segment was in a 100% coil conformation (pH 7.0) or in an 80% alpha-helical conformation (pH 10.3). At the higher pH, aggregates were smaller in size (hydrodynamic radius: 364 nm --> 215 nm) and chains were more densely packed at the core-corona interface (interchain distance: 3.2 nm --> 2.4 nm). Changes in size and structure could be explained in basic terms of colloid stabilization without considering a secondary structure effect.
Sigel
Reinhard
R
Max Planck Institute of Colloids and Interfaces, Colloid Chemistry, Research Campus Golm, 14424 Potsdam, Germany.
Łosik
Magdalena
M
Schlaad
Helmut
H
D002070:Butadienes / Q000737:chemistry*; D003102:Colloids; D020724:Elastomers / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D011107:Polylysine / Q000737:chemistry*; D011108:Polymers / Q000737:chemistry*; D017433:Protein Structure, Secondary
D002070:Butadienes; D003102:Colloids; D020724:Elastomers; D011108:Polymers; D011107:Polylysine; C028834:polybutadiene