Binding and release characteristics of insulin-like growth factor-1 from a collagen-glycosaminoglycan scaffold

Tissue engineering is a promising technique for cartilage repair, but to optimize novel scaffolds before clinical trials, it is necessary to determine their characteristics for binding and release of growth factors. Toward this goal, a novel, porous collagen-glycosaminoglycan scaffold was loaded with a range of concentrations of insulin-like growth factor-1 (IGF-1) to evaluate its potential as a controlled delivery device. The kinetics of IGF-1 adsorption and release from the scaffold was demonstrated using radiolabeled IGF-1. Adsorption was rapid, and was approximately proportional to the loading concentration. Ionic bonding contributed to this interaction. IGF-1 release was studied over 14 days to compare the release profiles from different loading groups. Two distinct phases occurred: first, a burst release of up to 44% was noted within the first 24 h; then, a slow, sustained release (13%-16%) was observed from day 1 to 14. When the burst release was subtracted, the relative percentage of remaining IGF-1 released was similar for all loading groups and broadly followed t(½) kinetics until approximately day 6. Scaffold cross-linking using dehydrothermal treatment did not affect IGF-1 adsorption or release. Bioactivity of released IGF-1 was confirmed by seeding scaffolds (preadsorbed with unlabeled IGF-1) with human osteoarthritic chondrocytes and demonstrating increased proteoglycan production in vitro.