Mechanistic aspects of blood-contacting properties of polypropylene surfaces--from the viewpoint of macromolecular entanglement and hydrophobic interaction via water molecules.
Polypropylene surfaces with a particular crystalline-amorphous microstructure have been demonstrated to reduce protein adsorption and platelet activation. Such blood-contacting properties may be affected by the crystalline-amorphous microstructure of the surfaces, although wettability such as dynamic contact angles and surface free energy components were almost constant, being independent from the variation in the microstructure. In order to clarify the mechanistic aspects on their blood-contacting properties, the physicochemical properties of the surfaces were evaluated for a series of compression-molded polypropylene sheets in terms of the work of adhesion and the structure of sorbed water. The work of adhesion of the compression-molded sheets increased with decreasing surface layer crystallinity, presumably due to macromolecular entanglement with a polymeric glue used. The work of adhesion involving macromolecular entanglement may occur between proteins and the surfaces. Thus, a decrease in the surface layer crystallinity is considered to cause an increase in the protein adsorption. The structure of water sorbed into the sheets changed--it was more gaseous (isolated) at the surfaces with a higher crystallinity. This suggests that the hydrophobic interaction via water molecules increased with surface layer crystallinity, resulting in increasing protein adsorption and denaturation. Thus, it is considered that both macromolecular entanglement and hydrophobic interaction are important on the mechanistic aspects of blood-contacting properties of polypropylene surfaces. In order to confirm this hypothesis, the evaluation of the physicochemical properties and blood-contacting properties was also performed on a series of uniaxially drawn polypropylene films. A decrease in the work of adhesion and the hydrophobic interaction at the surfaces was observed with increasing draw ratio, and the protein adsorption and platelet activation were effectively prevented with increasing draw ratio. This result supports our hypothesis. Therefore, it is concluded that the excellent blood-contacting properties of polypropylene surfaces can be achieved by reducing the macromolecular entanglement and the hydrophobic interaction with proteins.
Kawamoto
N
N
School of Materials Science, Japan Advanced Institute of Science and Technology, Ishikawa, Japan.
Mori
H
H
Yui
N
N
Terano
M
M
D000268:Adhesiveness; D000327:Adsorption; D000818:Animals; D001696:Biomechanical Phenomena; D001769:Blood / Q000378:metabolism*; D001792:Blood Platelets / Q000737:chemistry; D001798:Blood Proteins / Q000737:chemistry*; D003460:Crystallization; D015539:Platelet Activation; D011126:Polypropylenes / Q000737:chemistry*; D011489:Protein Denaturation; D011817:Rabbits; D013499:Surface Properties; D014867:Water / Q000737:chemistry*
D001798:Blood Proteins; D011126:Polypropylenes; D014867:Water