Supplementary Figure 3: Analysis of HSA-targeted nanobodies
From: Yeast surface display platform for rapid discovery of conformationally selective nanobodies
(a) Library design was assessed by monitoring the change in amino acid frequency in CDR3 throughout selection rounds with HSA as the antigen. Few changes were observed, with the only notable trend a modest increase in basic residue frequency and a decline in acidic residue frequency. (b) Assessment of Nb.b201 binding to human serum albumin by surface plasmon resonance, comparison with mouse serum albumin which shows no detectable binding. (c) 2Fo-Fc composite omit map contoured at 1.5 σ for antigen bound Nb.b201. The structure of both bound (yellow) and free (gray) forms of the nanobody are shown, highlighting structural divergence. (d) 2Fo-Fc composite omit map contoured at 1.5 σ for free Nb.b201.
