As a model system
to study the elasticity of bottle-brush polymers,
we here introduce self-assembled DNA bottle brushes, consisting of
a DNA main chain that can be very long and still of precisely defined
length, and precisely monodisperse polypeptide side chains that are
physically bound to the DNA main chains. Polypeptide side chains have
a diblock architecture, where one block is a small archaeal nucleoid
protein Sso7d that strongly binds to DNA. The other block is a net
neutral, hydrophilic random coil polypeptide with a length of exactly
798 amino acids. Light scattering shows that for saturated brushes
the grafting density is one side chain per 5.6 nm of DNA main chain.
According to small-angle X-ray scattering, the brush diameter is D = 17 nm. By analyzing configurations of adsorbed DNA bottle
brushes using AFM, we find that the effective persistence of the saturated
DNA bottle brushes is Peff = 95 nm, but
from force–extension curves of single DNA bottle brushes measured
using optical tweezers we find Peff =
15 nm. The latter is equal to the value expected for DNA coated by
the Sso7d binding block alone. The apparent discrepancy between the
two measurements is rationalized in terms of the scale dependence
of the bottle-brush elasticity using theory previously developed to
analyze the scale-dependent electrostatic stiffening of DNA at low
ionic strengths.