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. 2020 Oct 22;12(11):1004. doi: 10.3390/pharmaceutics12111004

Figure 1.

Figure 1

T22-GFP-H6 nanoparticle characterization. (A) Modular organization of T22-GFP-H6 protein building blocks. T22 is a CXCR4 specific cationic tag derivative of poliphemusin II protein from horseshoe crab [26]. L is a linker commonly used in phage display and H6 corresponds to polyhistidine architectonic tag. Relative length of the modules is only indicative. (B) Protein intrinsic fluorescence emission spectrum upon excitation at 450 nm wavelength. Red bar indicates fluorescence emission maximum at 510 nm. (C) In silico supramolecular organization model of protein building blocks into toroid-like nanoparticles. Each monomer is represented in a different color. Modified from [43] with permission of John Wiley and Sons. (D) Average molar mass distribution of T22-GFP-H6 nanoparticles determined by size exclusion chromatography coupled to multi angle light scattering (SEC-MALS).