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. Author manuscript; available in PMC: 2019 Dec 28.
Published in final edited form as: J Control Release. 2018 Oct 23;292:183–195. doi: 10.1016/j.jconrel.2018.10.026

Figure 1. A recombinant elastin-like polypeptide (ELP) fusion protein as a non-covalent drug carrier for cyclosporine A (CsA).

Figure 1.

A) A gene was constructed encoding the cyclophilin A protein fused to a high molecular weight ELP, A192. This fusion, called CA192, binds specifically and with high affinity to CsA; B) SDS-PAGE of purified CA192 (91.6 kDa) stained with copper chloride demonstrates a molecular weight shift upon fusing CypA to A192 (73.6 kDa); C) Optical density was determined as a function of temperature (1°C/min) for 25 μM CA192, free A192, and a PBS control. The temperature with the maximum positive slope was defined as the phase transition temperature. D) The concentration-temperature phase diagrams of both CA192 and A192 are plotted, showing that both are expected to remain soluble at physiological temperatures. The 95% confidence interval around each best-fit line is indicated with dashed lines.