Rapid binding of concanavalin A and maltose-polyrotaxane conjugates due to mobile motion of α-cyclodextrins threaded onto a poly(ethylene glycol)
Rapid binding of concanavalin A and maltose-polyrotaxane conjugates due to mobile motion of α-cyclodextrins threaded onto a poly(ethylene glycol)
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DOI:
10.1021/bc049809h
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发表时间:
2005-01-01
影响因子:
4.7
通讯作者:
Yui, N
中科院分区:
文献类型:
--
作者:
Ooya, T;Utsunomiya, H;Yui, N
Maltose-polyrotaxane conjugates (Mal-PRXs), in which maltose-conjugated alpha-cyclodextrins (alpha-CDs) are threaded onto a poly(ethylene glycol) (PEG) chain capped with benzyloxycarbonyl-L-tyrosine, were characterized in terms of their molecular motion and the relation to multivalent interactions between the maltose moiety and concanavalin A from Canavalia ensiformis (Con A). Spin-lattice relaxation time (T-1) and spin-spin relaxation time (T-2) of alpha-CD C(1), maltosyl C(1), and PEG methylene protons in the Mal-PRXs revealed that the mobile motion of alpha-CDs in the polyrotaxane governed the molecular motion of maltosyl groups in alpha-CDs and threading PEG chain. The association constant (K-a) of the Mal-PRXs with 22, 38 and 53% of alpha-CD threading was 5.7 x 10(4), 1.1 x 10(6), and 5.3 x 10(5) (M-1-maltose), respectively. The largest K. value of the Mal-PRX with 38% of alpha-CD threading was well correlated with the T-1 and T-2 values of maltosyl groups and alpha-CD, suggesting that the mobile motion of maltose-conjugated alpha-CDs in the Mal-PRX contributes to the highest affinity with Con A. Initial rate of binding with Con A was also governed by the mobile motion of maltose-conjugated alpha-CDs. Therefore, we concluded that both highly molecular motion due to the mobile motion of maltose-conjugated alpha-CDs and multivalency of the Mal-PRXs contributes to inducing rapid Con A binding.