Journal
ACS BIOMATERIALS SCIENCE & ENGINEERING
Volume 1, Issue 2, Pages 79-84Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ab500088b
Keywords
polymer-peptide conjugates; self-assembly; molecular dynamics; coiled coils; drug delivery
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Funding
- Office of Naval Research [N00014-13-1-0760]
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We investigate the conformations of multiple poly ethylene glycol (PEG) chains conjugated to the exterior surface of a three-helix coiled coil using all-atomistic molecular dynamics simulations in an explicit solvent. Our simulations indicate that the helical content and coiled coil configuration of the peptide assembly are preserved at low degrees of polymerization. We observe that the conjugated PEG chains form a mushroomlike protective shell around the coiled coil, where the scaling of radius of gyration of PEG with molecular weight further confirms minimal steric hindering between chains. Our simulations suggest that conjugation of low-molecular weight polymers to coiled coils at densities approaching one conjugate per heptad does not induce unfolding, and in contrast may be a viable means to further improve compatibility and stability in biomaterials and drug delivery applications.
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