To What Extent Does Surface Hydrophobicity Dictate Peptide Folding and Stability near Surfaces?
Protein-surface interactions are ubiquitous in both the cellular setting and in modern bioengineering devices, but how such interactions impact protein stability is not well understood. We investigate the folding of the GB1 hairpin peptide in the presence of self-assembled monolayers and graphite like surfaces using replica exchange molecular dynamics simulations. By varying surface hydrophobicity, and decoupling direct protein-surface interactions from water-mediated interactions, we show that surface wettability plays a surprisingly minor role in dictating protein stability. For both the β-hairpin GB1 and the helical miniprotein TrpCage, adsorption and stability is largely dictated by the nature of the direct chemical interactions between the protein and the surface. Independent of the surface hydrophobicity profile, strong protein-surface interactions destabilize the folded structure while weak interactions stabilize it.
Department of Chemical and Biomolecular Engineering, Lehigh University , Bethlehem, Pennsylvania 18015, United States.
Gül H
GH
Zerze
Department of Chemical Engineering, University of California , Santa Barbara, California 93106, United States.
Ryan G
RG
Mullen
Department of Chemistry and Biochemistry, University of California , Santa Barbara, California 93106, United States.|Department of Physics, University of California , Santa Barbara, California 93106.
Zachary A
ZA
Levine
Department of Chemistry and Biochemistry, University of California , Santa Barbara, California 93106, United States.|Department of Physics, University of California , Santa Barbara, California 93106.
Joan-Emma
JE
Shea
Department of Chemical and Biomolecular Engineering, Lehigh University , Bethlehem, Pennsylvania 18015, United States.
Jeetain
J
Mittal
D057927:Hydrophobic and Hydrophilic Interactions; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding; D013499:Surface Properties; D017155:Wettability
D010455:Peptides