Table 1.

Five designed ELP sequences for this study consist of three repeats of VPGXG with different guest residues to modify the hydrophobicity of the sequence

Peptide name	Molecular weight	Peptide sequence	Average hydrophilicity of full sequence	Average hydrophilicity based on different guest residues
ELPV3	2023.37	Ac-CGKLVPGVGVPGVGVPGVGGGGY-NH2	−0.48	a
ILELPV3	2249.69	Ac-CGKLVPGVGVPGVGVPGVGILGGGY-NH2	−0.59	−1.5
ILELPIV2	2263.71	Ac-CGKLVPGIGVPGVGVPGVGILGGGY-NH2	−0.60	−1.6
ILELPI2V	2277.74	Ac-CGKLVPGIGVPGIGVPGVGILGGGY-NH2	−0.61	−1.7
ILELPI3	2291.77	Ac-CGKLVPGIGVPGIGVPGIGILGGGY-NH2	−0.62	−1.8

A cysteine residue has been added to facilitate gold binding, and a tyrosine tag is conjugated as a redox-active amino acid to the C-terminal. The average hydrophilicity is calculated by Hopp & Woods’ hydrophilicity scale.

^aELPV3 has different flanking amino acids than the other peptides in this study so the average hydrophilicity was not calculated.