TY - JOUR
T1 - Versatility of thermosensitive particles
AU - Kawaguchi, H.
AU - Kisara, K.
AU - Takahashi, T.
AU - Achiha, K.
AU - Yasui, M.
AU - Fujimoto, K.
PY - 2000
Y1 - 2000
N2 - Poly(N-isopropylacrylamide) (PNIPAM) particles are highly swollen below the transition temperature in water so that they become very soft and hydrophilic, but collapsed above the transition temperature to become hard and hydrophobic. Such changes bring about the discontinuous temperature dependence of adsorbability of protein, activity of immobilized enzyme, cell activating ability of the particles. The transition temperature of PNIPAM was changed by binding something to the chain end and this property was used to control the enzyme activity with temperature. Sudden change in the topology of the particle surface by quick temperature change gave excess stimulus to cells when the change was transmitted straightly to the cells.
AB - Poly(N-isopropylacrylamide) (PNIPAM) particles are highly swollen below the transition temperature in water so that they become very soft and hydrophilic, but collapsed above the transition temperature to become hard and hydrophobic. Such changes bring about the discontinuous temperature dependence of adsorbability of protein, activity of immobilized enzyme, cell activating ability of the particles. The transition temperature of PNIPAM was changed by binding something to the chain end and this property was used to control the enzyme activity with temperature. Sudden change in the topology of the particle surface by quick temperature change gave excess stimulus to cells when the change was transmitted straightly to the cells.
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U2 - 10.1002/1521-3900(200002)151:1<591::AID-MASY591>3.0.CO;2-P
DO - 10.1002/1521-3900(200002)151:1<591::AID-MASY591>3.0.CO;2-P
M3 - Article
AN - SCOPUS:0033653170
SN - 1022-1360
VL - 151
SP - 591
EP - 598
JO - Macromolecular Symposia
JF - Macromolecular Symposia
ER -