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Manipulation of unfolding-induced protein aggregation by peptides selected for aggregate-binding ability through phage display library screening

, : Manipulation of unfolding-induced protein aggregation by peptides selected for aggregate-binding ability through phage display library screening. Biochemical and Biophysical Research Communications 291(4): 903-907

A phage-displayed library of peptides (12-mer) was screened for the ability to bind to thermally aggregated bovine carbonic anhydrase (BCA), with a view toward examining whether peptides possessing this ability might bind to partially structured intermediates on the protein's unfolding pathway and, therefore, constitute useful tools for manipulation of the kinetic partitioning of molecules between the unfolded and aggregated states. Two peptides (N-HPST-MGLRTMHP-C and N-TPSAWKTALVKA-C) were identified and tested. While neither showed thermal aggregation autonomously, both peptides individually elicited remarkable increases in the levels of thermal aggregation of BCA. A possible explanation is that both peptides bind to surfaces on molten BCA that are not directly involved in aggregation. Such binding could slow down interconversions between folded and unfolded states and states and stabilize aggregation-prone intermediate(s) to make them more prone to aggregation, while failing to achieve any steric prevention of aggregation. The approach has the potential of yielding useful aggregation-aiding/inhibiting agents, and may provide clues to whether amorphous aggregates are "immobilized" forms of folding intermediates.


PMID: 11866450

DOI: 10.1006/bbrc.2002.6549

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