J. Ericsson et al., SYNTHESIS OF HYDROPHILIC POLY(VINYL ETHER)S AND THEIR APPLICATION FORSEPARATION MEDIA DESIGN, Reactive & functional polymers, 30(1-3), 1996, pp. 327-340
Poly(2-acetoxyethyl vinyl ether (AcOVE)) and poly(2-acetoxyethyl vinyl
ether-co-2-vinyloxyethyl phthalimide) were synthesized by traditional
cationic polymerization, typically at -20 degrees C in toluene with B
F3O(C2H5)(2) as initiator, to give polymers with degrees of polymeriza
tion (Dp) in the range of 600-1100. In addition, poly(AcOVE) was polym
erized by controlled cationic polymerization at 0 degrees C with molec
ular weights in a predetermined fashion. The Dp's were calculated from
Dp = [M](0)/[I](0) and typical values were 5, 10, 100 and 200. The mo
lecular weight values obtained for a theoretical Dp = 200, were for po
ly(2-acetoxyethyl vinyl ether), M(n) = 19,200, M(w) = 22,700 and polyd
ispersity = 1.2, as determined by GPC. The deprotected hydrophilic pol
ymers, poly(2-hydroxyethyl vinyl ether) and poly(2-hydroxyethyl vinyl
ether-co-2-aminoethyl vinyl ether), were used for the preparation of n
ovel gel filtration media as well as new anion exchangers. In the case
of gel filtration, poly(2-hydroxyethyl vinyl ether) was attached to a
beaded agarose matrix (34 mu m), i.e. Sepharose(R) HP. It was shown t
hat the attachment of the poly(vinyl ether) affected the selectivity.
In gel filtration of selected biomolecules, the poly(vinyl ether) modi
fied agarose matrix showed performance characteristics comparable to t
he reference used, i.e. Superdex(R) 30 prep grade. In addition the pol
y(vinyl ether)s were shown to be stable in a wide pH-range. The stabil
ity was confirmed by the conclusion that no changes in molecular weigh
t were observed after treatment with 0.1 M HCl (pH = 1) or 0.01 M NaOH
(pH = 12) for six weeks at 40 degrees C. For the preparation of anion
-exchanger media, the beads containing poly(2-hydroxyethyl vinyl ether
) was further modified with a quaternary ammonium group, to produce a
separation media having a high dynamic binding capacity for bovine ser
um albumin (BSA).