Although the TACC3/Aurora-A interaction lacks a defined secondary structure, TACC3 becomes more ordered on binding to Aurora-A. We, therefore, explored the use of a maleimide crosslinker to constrain the cysteine variants of the WT peptide between the i and i+3 positions to limit the conformational landscape of the peptide and perhaps favor formation of the 310-helical turn observed in the crystal structure (Table ; supporting Fig. ). These variants did not lead to enhanced inhibitory potency (Table , Fig. ).