(16h) Protein Adsorption on Phospholipid Polymer Interfaces: The Effect of Chain Length and Its Hydration Structure | AIChE

(16h) Protein Adsorption on Phospholipid Polymer Interfaces: The Effect of Chain Length and Its Hydration Structure

Authors 

Shimanouchi, T. - Presenter, Okayama University
Kimura, Y., Okayama University
Nakayama, T., Okayama University

“‡“à‹v”üŽq “‡“à‹v”üŽq 5 222 2019-04-12T14:27:00Z 2019-04-12T14:50:00Z 1 497 2836 23 6 3327 14.00

Clean Clean false 0 2 false false false EN-US JA X-NONE


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text-indent:15.75pt;mso-char-indent-count:1.5">The
biocompatible materials demands the low affinity to proteins in the field of
artificial organs or biosensor. Therefore, the polymer with similar chemical structure
to the biomembrane is a promising materials. Some reserchers have developed the
materials such as poly(2-methacryloyloxyethyl phosphorylcholine)
(PMPC). These maetrilas could give the prominent property regarding the low
affinity to proteins. It is probable that this property results from the steric
effect due to the polymer chain layer between the interface and the solid
surface and the hydration structure of polymers [1]. However, these results has been limited to the specific proteins such
as albumin. For the generalization, the protein adsorption behavior should be
discussed in terms of its surface property. In this study, we prepared the PMPC
with different chain length to clarify the effect of protein adsorption. The
surface of PMPC interfaces were observed with an atomic force microscopy (AFM) under
the air and liquid conditions. Six kinds of proteins were used to reveal the
effect of surface property of peotein on the adsorption
behavior. Finally, we discussed the relationship between the outcomes obtained
from AFM observations and the protein adsorption behavior.

text-indent:15.75pt;mso-char-indent-count:1.5">Phosphorylcholine self-assembled monolayers (PC-SAM) and
poly(2-methacryloyloxyethyl phosphorylcholine) (PMPCn; n = 10, 50, and 100) were
used in this study. PC-SAM, PMPC10, PMPC50, and PMPC100 were synthesized
according to the previous report [1]. Six kinds of proteins were used for the test
of their adsoption behavior 10.5pt;font-family:" times new roman>: amyloid beta, apolipoprotein A-I,
a-synuclein, lysozyme, bovine serum albumin, and insulin.

text-indent:15.75pt;mso-char-indent-count:1.5">In the
first, we examined the effect of chain length of PMPC on the interface. Their
surface state was observed with an atomic force microscopy under the air and
liquid conditions. The roughness was 3 nm under the air condition nevertheless to
the chain length. In contrast, the large variation of roughness was observed
under the liquid condition. PMPC100 indicated the large roughness higher than
that under the air condition. This is because the chains of PMPC100
longitudinaly fluctuated on the solid substrate. AFM observations suggested
that the enegy dissipation at the interface was related with the hydration at
the interface.

text-indent:15.75pt;mso-char-indent-count:1.5">Nest,
we measured the adhesive force of tip of canti lever
in AFM system to the PMPC interfaces, normal">Fadh.
The Fadh
" times new roman>value decreased with the increase in chain length of
PMPC. The decrease in normal">Fadh
" times new roman>value was likely to result from the energy
dissipation or hydration at the interface. The
adsorption property of PMPC interfaces towards the proteins was examined by the
quartz crystal microbalance method. Overall, the PC-SAM indicated higher amount
than other membranes. Also, the proteins such as Ab,
insulin, and font-family:Symbol">a font-family:" times new roman>-synuclein indicated the higher amount
than other types of proteins. The absorbed amount of proteins to PMPC
interfaces was plotted against the corresponding normal">Fadh value. In any protein, the linear relationship
between both was observed. The normal">Fadh value was corrected with the surface properties
of proteins such as their hydrophobicity. Thereby, the corrected Fadh values
could be correlated with the adsorbed amount of protiens to the PMPC intrfaces.

text-indent:15.75pt;mso-char-indent-count:1.5">

[1]
D.Nagasawa et al., J. Phys Chem. C, 119,
17193-17201(2015)