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. 2016 May 23;72(Pt 6):434–442. doi: 10.1107/S2053230X16007202

Figure 4.

Figure 4

Alternative linking strategies. The left column indicates the modification. The middle column shows the superposition of each Fab–alternative cyclic peptide complex (colored C atoms) on the Fab–acetylated-amidated disulfide peptide (white C atoms). The right column is the corresponding SPR trace. In all cases, the linking atoms are shifted away from the Val9/Ile10 residues and thus do not pack as well. The affinity of the aminoheptanoic acid linker (AHA) was the closest to the original disulfide meditope.