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. Author manuscript; available in PMC: 2013 Sep 9.

Published in final edited form as: Soft Matter. 2012 Aug 14;8(30):7909–7918. doi: 10.1039/C2SM25779C

Binding of CRP-LPP mimics to immobilized C1q by ELISA. Purified human C1q (1 μg/mL) was coated on ELISA plates and the plates were incubated at increasing concentrations with each CRP-LPP mimic: 21 nm ( ), 26 nm ( ), 28 nm ( ), 41 nm ( ), 64 nm ( ), and PC liposome (□). The degree of mCRP binding was detected using biotinylated polyclonal anti-CRP antibody. The measured absorbance was normalized to a BSA blank control. (a) Concentration-dependent binding of CRP-LPP mimic to C1q. Inset: C1q binding of the pCRP (×) and mCRP (○) controls. (b) Binding of CRP-LPP mimics (1.8 μg/mL CRP) to C1q. Data represents mean absorbance ±SD, n = 3. ** p<0.01; ***p<0.001 compared to pCRP.

Inline graphic — Binding of CRP-LPP mimics to immobilized C1q by ELISA. Purified human C1q (1 μg/mL) was coated on ELISA plates and the plates were incubated at increasing concentrations with each CRP-LPP mimic: 21 nm ( ), 26 nm ( ), 28 nm ( ), 41 nm ( ), 64 nm ( ), and PC liposome (□). The degree of mCRP binding was detected using biotinylated polyclonal anti-CRP antibody. The measured absorbance was normalized to a BSA blank control. (a) Concentration-dependent binding of CRP-LPP mimic to C1q. Inset: C1q binding of the pCRP (×) and mCRP (○) controls. (b) Binding of CRP-LPP mimics (1.8 μg/mL CRP) to C1q. Data represents mean absorbance ±SD, n = 3. ** p<0.01; ***p<0.001 compared to pCRP.