In vitro reconstitution of fibrillar collagen type I assemblies at reactive polymer surfaces.
The reconstitution of fibrillar collagen and its assemblies with heparin and hyaluronic acid was studied in vitro. Fibril formation kinetics were analyzed by turbidity and depletion measurements in solutions containing varied concentrations of collagen and glycosaminoglycans. Fibril-forming collagen solutions were further applied for the coating of planar substrates which had been modified with alternating maleic anhydride copolymer films before. The immobilized collagen assemblies were characterized with respect to the deposited amount of protein using ellipsometry and acidic hydrolysis/HPLC-based amino acid analysis, respectively. AFM, SEM, and cLSM were utilized to gain information on structural features and patterns formed by surface-attached fibrils depending on the initial solution concentrations of collagen. The results revealed that the addition of heparin and hyaluronic acid affected both the fibril dimensions and the meshwork characteristics of the surface-bound fibrils.
Salchert
Katrin
K
Institute of Polymer Research Dresden & The Max Bergmann Center of Biomaterials Dresden, Hohe Strasse 6, 01069 Dresden, Germany.
Streller
Uwe
U
Pompe
Tilo
T
Herold
Nicole
N
Grimmer
Milauscha
M
Werner
Carsten
C
D000596:Amino Acids / Q000737:chemistry; D015374:Biosensing Techniques / Q000379:methods; D024042:Collagen Type I / Q000032:analysis* / Q000737:chemistry*; D005782:Gels; D006025:Glycosaminoglycans / Q000737:chemistry; D055767:Immobilized Proteins; D007700:Kinetics; D009391:Nephelometry and Turbidimetry / Q000379:methods; D011108:Polymers / Q000737:chemistry*; D013499:Surface Properties
D000596:Amino Acids; D024042:Collagen Type I; D005782:Gels; D006025:Glycosaminoglycans; D055767:Immobilized Proteins; D011108:Polymers