Fibrillogenesis in continuously spun synthetic collagen fiber

• Published in: Journal of biomedical materials research. Part B, Applied biomaterials Vol. 93B; no. 1; pp. 24 - 38
• Main Authors: Caves, Jeffrey M., Kumar, Vivek A., Wen, Jing, Cui, Wanxing, Martinez, Adam, Apkarian, Robert, Coats, Julie E., Berland, Keith, Chaikof, Elliot L.
• Format: Journal Article
• Language: English
• Published: Hoboken Wiley Subscription Services, Inc., A Wiley Company 01.04.2010
• Subjects: Animals; Biocompatible Materials - chemical synthesis; Biocompatible Materials - chemistry; Biomechanical Phenomena; Calorimetry, Differential Scanning; collagen fiber; Cross-Linking Reagents; fibril; Fibrillar Collagens - chemical synthesis; Fibrillar Collagens - chemistry; Fibrillar Collagens - ultrastructure; fibrillogenesis; Glutaral; Male; Materials Testing; Mice; Mice, Inbred C57BL; Microscopy, Electron, Transmission; Molecular Structure; Prostheses and Implants; Protein Multimerization; Rats; self-assembly; Tensile Strength; wet spinning
• ISSN: 1552-4973; 1552-4981; 1552-4981
• DOI: 10.1002/jbm.b.31555

The universal structural role of collagen fiber networks has motivated the development of collagen gels, films, coatings, injectables, and other formulations. However, reported synthetic collagen fiber fabrication schemes have either culminated in short, discontinuous fiber segments at unsuitably low production rates, or have incompletely replicated the internal fibrillar structure that dictates fiber mechanical and biological properties. We report a continuous extrusion system with an off‐line phosphate buffer incubation step for the manufacture of synthetic collagen fiber. Fiber with a cross‐section of 53± 14 by 21 ± 3 μm and an ultimate tensile strength of 94 ± 19 MPa was continuously produced at 60 m/hr from an ultrafiltered monomeric collagen solution. The effect of collagen solution concentration, flow rate, and spinneret size on fiber size was investigated. The fiber was further characterized by microdifferential scanning calorimetry, transmission electron microscopy (TEM), second harmonic generation (SHG) analysis, and in a subcutaneous murine implant model. Calorimetry demonstrated stabilization of the collagen triple helical structure, while TEM and SHG revealed a dense, axially aligned D‐periodic fibril structure throughout the fiber cross‐section. Implantation of glutaraldehyde crosslinked and noncrosslinked fiber in the subcutaneous tissue of mice demonstrated limited inflammatory response and biodegradation after a 6‐week implant period. © 2009 Wiley Periodicals, Inc. J Biomed Mater Res Part B: Appl Biomater, 2010