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. Author manuscript; available in PMC: 2010 Jul 24.

Published in final edited form as: Adv Funct Mater. 2009 Jul 24;19(14):2325–2331. doi: 10.1002/adfm.200900107

(A) bFGF loading/absorption into 10wt% PEG-10kDa hydrogels (dotted bar) or PEG gels functionalized with KRTGQYKL (white bars) or scrambled KGRYQKTL peptide (gray bars). Asterisks designate statistical significance compared to unmodified PEG hydrogels as per Students’ T-test (N=3, Mean ± SEM; p<0.05) (B) Sustained release of bFGF from affinity peptide (KRTGQYKL) functionalized PEG hydrogels (10 kDa, 10 wt%). bFGF was encapsulated (750 ng/gel) in PEG hydrogels in situ during photopolymerization with different affinity peptide concentrations and architecture. R=0 (⋄); 100 (△) 1000 (○); Semi-IPN, R=50 (×). (N=3, mean ± SEM)

(A) bFGF loading/absorption into 10wt% PEG-10kDa hydrogels (dotted bar) or PEG gels functionalized with KRTGQYKL (white bars) or scrambled KGRYQKTL peptide (gray bars). Asterisks designate statistical significance compared to unmodified PEG hydrogels as per Students’ T-test (N=3, Mean ± SEM; p<0.05) (B) Sustained release of bFGF from affinity peptide (KRTGQYKL) functionalized PEG hydrogels (10 kDa, 10 wt%). bFGF was encapsulated (750 ng/gel) in PEG hydrogels in situ during photopolymerization with different affinity peptide concentrations and architecture. R=0 (⋄); 100 (△) 1000 (○); Semi-IPN, R=50 (×). (N=3, mean ± SEM)