Lotus-Leaf-Like Topography Predominates over Adsorbed ECM Proteins in Poly (3-hydroxybutyrate-co-3-hydroxyhexanoate) Surface/Cell Interactions
Jun Zheng †‡（郑军）,Dan Li†*（李丹）, Lin Yuan†（袁琳）,Xiaoli Liu†（刘小莉）,Hong Chen†*（陈红）
† Jiangsu Key Laboratory of Advanced Functional Polymer Design and Application, The Key Lab of Health Chemistry and Molecular Diagnosis of Suzhou, College of Chemistry, Chemical Engineering and Materials Science, Soochow University, Suzhou 215123, People′s Republic of China
‡ School of Materials Science and Engineering, Wuhan University of Technology, Wuhan 430070, People′s Republic of China
ACS Appl. Mater. Interfaces 2013, 5, 5882−5887.
It is well-known that extracellular matrix (ECM) proteins mediate cell/surface interactions. However, introduction of a specific surface topography may disturb the correlation between ECM proteins adsorption and cells adhesion on a given surface. In present study, lotus-leaf-like topography was introduced on the surface of a biodegradable material, poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) (PHBHHx). Protein adsorption and cell interactions with this lotus-leaf-like surface (designated PHBHHx-L) were investigated. Water contact angle data indicated that the hydrophobicity of PHBHHx was enhanced by the introduction of lotus-leaf-like topography. The adsorption of extracellular matrix proteins (fibronectin and vitronectin) on PHBHHx-L was measured by enzyme linked immunosorbent assay (ELISA). Compared with flat PHBHHx, adsorption on the PHBHHx-L surface increased by 260% for fibronectin and 40% for vitronectin. In contrast, fibroblast and endothelial cell adhesion and proliferation were reduced on the PHBHHx-L compared to the flat polymer surface. These results suggest that the inhibition of cell adhesion and proliferation caused by the lotus-leaf-like topography dominates over the effect of the adsorbed adhesive proteins in promoting adhesion and proliferation. It can be concluded that the lotus-leaf-like topography plays a dominant role in cell/PHBHHx-L interactions. The present findings indicate the complexity of the interplay among surface topography, adsorbed proteins, and cell–surface interactions.
