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Diblocks of Elastin-like Polypeptides Form Weak Micelles

Diblock copolymers
in
selective solvents self-assemble
in
aggregates,
called micelles. The
insoluble
blocks aggregate in the
micellar core,
protected by corona formed by stretched solvated blocks.
The structure
of elastin-like
polypeptide
(ELP) repeat
unit
suggests
that
surface tension at the core-corona boundary
could
be
considerably reduced compared to surface tension in conventional micelles
formed by synthetic copolymers.
Diblock copolymers
with  surface tension below thermal
energy
kT per chain
and with relatively
short
blocks
form
novel micelles with
almost
unstretched coronas.  The
theoretical
predictions are in good agreement with experimental observations of the
micellization
temperature and hydrodynamic
radius
of
the micelles
that
is
consistent
with the
unstretched
state of
corona
blocks.
This study is important 
for
the design of
polypeptide
carriers with desired
size
and properties
.