Protein unfolding leads to aggregation and loss of function. To monitor protein unfolding at low concentrations or in the presence of other folded proteins, we aim to develop antibodies specific for unfolded proteins. We posit that antibodies specific for solvent-exposed aromatic residues (which are normally solvent-shielded within folded proteins) will selectively recognize unfolded conformations of diverse proteins. Based on this hypothesis, we find that the complementarity determining regions of small antibodies can be engineered to selectively recognize unfolded proteins via pi-stacking interactions. We will discuss how these novel antibodies can be used to monitor protein unfolding in a highly sensitive and site-specific manner.

Design of antibodies specific for unfolded proteins

243rd National Meeting (2012)

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