Data from: Modulating peptide co-assembly via macromolecular crowding: Recipes for co-assembled structures

Peptide-based biomaterials are commonly found in applications such as
tissue engineering, wound healing, and drug delivery. Control over the
size and morphology of the peptide supramolecular structure remains a
challenge. One way to influence peptide assembly is through macromolecular
crowding. Here we use discontinuous molecular dynamics simulation combined
with the PRIME20 force field to investigate the effect of hydrophobic
crowders on the architecture of co-assembled peptide aggregates. The
peptide system used in this work is a mixture of oppositely-charged
synthetic peptides: “CATCH(6K+)” (KQKFKFKFKQK) and “CATCH(6E-)”
(EQEFEFEFEQE). The systems explored contained a mixture of 50 CATCH(6K+)
and 50 CATCH (6E-) peptides at peptide concentrations of 5 mM and 20 mM,
and crowders with diameters of 10, 20, 40 and 80 Å. Crowders were modeled
as spheres with either hard-sphere or square-well/square-shoulder
interactions. At low concentrations where CATCH co-assembly typically does
not occur, the crowders were effective chaperones to trigger co-assembly.
Small hard-sphere crowders promoted formation of multilayer fibrils. Large
highly hydrophobic crowders promoted the formation of monolayer β-sheet
structures and suppressed the formation of fibril structures. Overall, the
simulations demonstrate that the crowder size and crowder-sidechain
interaction strength govern the supramolecular architecture of peptide
co-assemblies.