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 occu..., , , # Dataset from Modulating peptide co-assembly via macromolecular crowding: Recipes for co-assembled structures

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Modulating peptide co-assembly via macromolecular crowding: Recipes for co-assembled structures. *Nanoscale*

This directory contains the results from coarse-grained discontinuous molecular dynamics (PRIME20/DMD) simulations for the investigating the impact of macromolecular crowding on peptide co-assembly.

## General overview of data included

Coordinate files from simulations are archived and compressed using tar and gzip.

| tarball name | description |
| ------------------- | --------------------------------------------------------------------------------------------------------------------------------- |
| 6K6E\_DMD.tar.gz | contains results and files relating to PRIME20/DMD simulations for systems of CATCH(6K/6E) peptides in the *absence* ...