469206 Exploring the Effects and Interplay of Elastin-like Polypeptide (ELP) Charge and Hydrophobicity on Mcherry-ELP Fusion Protein Self-Assembly
In this work, we systematically explored the impact of the charge and hydrophobicity of the coil-like ELP on fusion protein self-assembly. This was achieved by varying the composition of amino acids in the ELP pentapeptide repeat sequence—Xaa-Pro-Gly-Yaa-Gly (XPGYG)—in which the first position, Xaa, can be either valine (V) or isoleucine (I), with isoleucine being more hydrophobic, and the fourth position, Yaa, can be any amino acid except proline. In this work, we used a five pentapeptide repeat sequence that varied hydrophobicity by tuning the I/V content in the first position and phenylalanine (F)/V content in the fourth position. Additionally, three different charge states (neutral, negatively charged, and zwitterionic) were studied by changing some of the amino acids in the fourth position to lysine (K) and/or glutamic acid (E). Combination of all possible permutations of charge and hydrophobicity generated 9 ELP sequences that were then fused to mCherry via genetic engineering. The self-assembly of these systems was studied using small-angle X-ray scattering (SAXS), atomic force microscopy (AFM), and light scattering.
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