The model generated in this work utilized standard homology modeling methods and incorporated previous secondary structure prediction information for the KAP5-1 sequence. The N-terminal domain of KAP5-1 is predicted to be partially disordered, followed by multiple glycine and cysteine repeat domains . Comparative structural models available for KAP5-1 are only able to model the two glycine-rich domains, corresponding to residues 60-121 and 171-207 of the KAP5-1 sequence, with a minimum sequence identity of > 40 % . For both domains, the template structure is the snow flea antifreeze protein. For the c-terminal region multiple models are available, ranging from tandem repeat to globular domains, but with a lower sequence identity. We attempted to model the C-terminal region, but no known similar sequences were found by BLAST search . This suggests superposition of the full length KAP5-1 sequence onto a model β-sheet, as done by Natarajan and Robbins, may not reflect the true 3D structure. With this information in mind, we chose to use a sequence truncated to only the regions with high sequence overlap with a known protein structure that reproduces the layer thickness, while simultaneously optimizing the positions of multiple cysteine residues on the outward loop region to increase the number of attachment sites for 18-MEA (cf. Figure ). Our model has the same secondary structural features as the Natarajan and Robbins' model, but was optimized based on sequence alignment and modeling against a known protein structure with the same glycine rich repeat motif (Supplemental Figure ).