Telechelic proteins form hydrogels through association of coiled-coil domains that flank flexible, hydrophilic central domains.  The coiled-coil domains associate into clusters that are similar to those formed by the individual coiled-coils; the central domains remain soluble and provide elastic connections between the coiled-coil network junctions. Unfolding of the coiled coils with pH, temperature, ionic strength, or protein denaturants can be used to trigger the gel-to-sol transition by weakening interchain interactions. Because the coiled-coil strand exchange time is the predominant factor governing the relaxation time of the protein hydrogels, viscoelastic behavior can be programmed at the genetic level.  This lecture will examine the structural and dynamic properties of artificial protein hydrogels and their origins in the primary sequences of the constituent proteins.

Programmed assembly of artificial protein hydrogels

243rd National Meeting (2012)

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