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Integrin α5β1‐mediated attachment of NIH/3T3 fibroblasts to fibronectin adsorbed onto electrospun polymer scaffolds
Author(s) -
Regis Shawn,
Youssefian Sina,
Jassal Manisha,
Phaneuf Matthew,
Rahbar Nima,
Bhowmick Sankha
Publication year - 2014
Publication title -
polymer engineering and science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.503
H-Index - 111
eISSN - 1548-2634
pISSN - 0032-3888
DOI - 10.1002/pen.23809
Subject(s) - fibronectin , scaffold , polycaprolactone , adsorption , tissue engineering , adhesion , protein adsorption , cell adhesion , materials science , ligand (biochemistry) , hydrolysis , biophysics , chemistry , polymer chemistry , receptor , cell , polymer , biomedical engineering , biochemistry , organic chemistry , composite material , medicine , biology
Protein adsorption and receptor‐ligand binding are two key first steps in the cell adhesion process. The ability to predetermine the success or failure of these processes would significantly advance the field of tissue engineering. This study examines fibronectin adsorption on functionalized electrospun polycaprolactone (PCL) scaffolds and determines the affinity of cell receptors for the adsorbed fibronectin onto each scaffold. After determining the affinity values, model plots were developed for each scaffold type based on the amount of fibronectin on the surface of the scaffold. The ability to theoretically predict the level of cell binding to a tissue engineering scaffold would significantly impact the decision of what scaffold type to use for a specific application. Results show that aminated PCL scaffolds adsorb significantly more protein than hydrolyzed PCL scaffolds; however, greater α5β1–fibronectin binding occurs on the hydrolyzed scaffolds. This is attributed to a higher affinity between the receptors on the cell and the fibronectin adsorbed onto hydrolyzed scaffolds compared with aminated scaffolds., POLYM. ENG. SCI., 54:2587–2594, 2014. © 2013 Society of Plastics Engineers