We discuss a simulation approach to understanding the behavior of mobile but surface-tethered peptides that are functionalized with polymers.  Such systems mimic the behavior of peptide amphiphiles in which polymers are used to stabilize folded peptide helical states that prevent undesired peptide-peptide interactions and assembly into beta-sheet structures.  We use a novel coarse-graining technique to develop simple models that recapitulate the basic and assembly driving forces.  Simulations show that functionalization with polymers can stabilize helical states, but the behavior is highly dependent on the specific amino acid at which the polymer is attached.  In some cases, polymer functionalization can destabilize the fold and actually promote aggregation.  We show that these unexpected results are actually well-understood in terms of a simple theory that accounts for the entropy of a polymer near an impenetrable surface.

Thermodynamics of surface-tethered peptide-polymer conjugates

249th National Meeting (2015)

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