TY - JOUR
T1 - Evaluation of Factors To Determine Platelet Compatibility by Using Self-Assembled Monolayers with a Chemical Gradient
AU - Sekine, Taito
AU - Tanaka, Yusaku
AU - Sato, Chikako
AU - Tanaka, Masaru
AU - Hayashi, Tomohiro
N1 - Publisher Copyright:
© 2015 American Chemical Society.
PY - 2015/6/30
Y1 - 2015/6/30
N2 - Intercorrelation among surface chemical composition, packing structure of molecules, water contact angles, amounts and structures of adsorbed proteins, and blood compatibility was systematically investigated with self-assembled monolayers (SAMs) with continuous chemical composition gradients. The SAMs were mixtures of two thiols: n-hexanethiol (hydrophobic and protein-adsorbing) and hydroxyl-tri(ethylene glycol)-terminated alkanethiol (hydrophilic and protein-resistant) with continuously changing mixing ratios. From the systematic analyses, we found that protein adsorption is governed both by sizes of proteins and hydrophobic domains of the substrate. Furthermore, we found a clear correlation between adsorption of fibrinogen and adhesion of platelets. Combined with the results of surface force measurements, we found that the interfacial behavior of water molecules is profoundly correlated with protein resistance and antiplatelet adhesion. On the basis of these results, we conclude that the structuring of water at the SAM-water interface is a critical factor in this context.
AB - Intercorrelation among surface chemical composition, packing structure of molecules, water contact angles, amounts and structures of adsorbed proteins, and blood compatibility was systematically investigated with self-assembled monolayers (SAMs) with continuous chemical composition gradients. The SAMs were mixtures of two thiols: n-hexanethiol (hydrophobic and protein-adsorbing) and hydroxyl-tri(ethylene glycol)-terminated alkanethiol (hydrophilic and protein-resistant) with continuously changing mixing ratios. From the systematic analyses, we found that protein adsorption is governed both by sizes of proteins and hydrophobic domains of the substrate. Furthermore, we found a clear correlation between adsorption of fibrinogen and adhesion of platelets. Combined with the results of surface force measurements, we found that the interfacial behavior of water molecules is profoundly correlated with protein resistance and antiplatelet adhesion. On the basis of these results, we conclude that the structuring of water at the SAM-water interface is a critical factor in this context.
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U2 - 10.1021/acs.langmuir.5b01216
DO - 10.1021/acs.langmuir.5b01216
M3 - Article
C2 - 26037132
AN - SCOPUS:84933567187
SN - 0743-7463
VL - 31
SP - 7100
EP - 7105
JO - Langmuir
JF - Langmuir
IS - 25
ER -