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This work focused on considering the cellular responses of the growth and differentiation of myoblasts, C2C12, on fibrillated collagen-coated poly(ε-caprolactone) (PCL) surfaces. Through a fibrillation processing window using NaCl and collagen weight fractions, collagen fibril coating density can be controlled. Three different collagen-fibril densities coated on PCL strut were used to investigate the effects of the collagen fibril on the myoblast activities. After physical and cellular analyses of the scaffolds, such as surface morphology, fibronectin absorption, wettability, and mechanical properties, the rate of cell growth and the proficiency of the myoblasts to develop skeletal myotubes were evaluated. Based on the results, although the coated collagen nanofibers were randomly distributed, the fibrillated collagen layer with the appropriate density on the PCL surface promoted a greater myotube formation than that of the control, which had no fibrillated collagen. In particular, relatively higher densities of collagen fibril showed significantly greater myotube formation than those of the control (not-fibrillated collagen-coated on the PCL surface) and lower density of collagen fibril.
This article was published in the following journal.
Name: Colloids and surfaces. B, Biointerfaces
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Autosomal dominant COLLAGEN DISEASES resulting from defective biosynthesis of COLLAGEN TYPE I and characterized by brittle, osteoporotic, and easily fractured bones. It may also present with blue sclerae, loose joints, and imperfect dentin formation. There are four major types, I-IV.
A fibrillar collagen found widely distributed as a minor component in tissues that contain COLLAGEN TYPE I and COLLAGEN TYPE III. It is a heterotrimeric molecule composed of alpha1(V), alpha2(V) and alpha3(V) subunits. Several forms of collagen type V exist depending upon the composition of the subunits that form the trimer.
A fibril-associated collagen usually found crosslinked to the surface of COLLAGEN TYPE II fibrils. It is a heterotrimer containing alpha1(IX), alpha2(IX) and alpha3(IX) subunits.
A fibrillar collagen found primarily in interstitial CARTILAGE. Collagen type XI is heterotrimer containing alpha1(XI), alpha2(XI) and alpha3(XI) subunits.
Large, multinucleate single cells, either cylindrical or prismatic in shape, that form the basic unit of SKELETAL MUSCLE. They consist of MYOFIBRILS enclosed within and attached to the SARCOLEMMA. They are derived from the fusion of skeletal myoblasts (MYOBLASTS, SKELETAL) into a syncytium, followed by differentiation.