Journal
MACROMOLECULES
Volume 53, Issue 16, Pages 6767-6779Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.macromol.9b02715
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Funding
- National Science Foundation MRSEC Grant [DMR 1720256]
- NSF EAGER [1508717]
- NSF Graduate Research Fellowship [1650114]
- Department of Energy [DE-FG02-87ER-45331]
- Office of Science, Office of Basic Energy Sciences of the U.S. Department of Energy [DE-AC02-05CH11231]
- NSF [CNS-1725797, MCB-1716956]
- Center for Scientific Computing from the CNSI, MRL: an NSF MRSEC [DMR-1720256]
- Extreme Science and Engineering Discovery Environment - XSEDE - NSF [TG-MCA05S027, ACI-1053575]
- Directorate For Engineering [1508717] Funding Source: National Science Foundation
- Div Of Chem, Bioeng, Env, & Transp Sys [1508717] Funding Source: National Science Foundation
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Ensembles of amino acid side chains often dominate the interfacial interactions of intrinsically disordered proteins; however, backbone contributions are far from negligible. Using a combination of nanoscale force measurements and molecular dynamics simulations, we demonstrated with analogous mussel-mimetic adhesive peptides and peptoids both 34 residues long that highly divergent adhesive/cohesive outcomes can be achieved on mica surfaces by altering backbone chemistry only. The Ph; Tyr, and Dopa containing peptoid variants used in this study deposited as dehydrated and incompressible films that facilitated analysis of peptoid side chain contributions to adhesion and cohesion. For example, whereas Phe and Dopa peptoids exhibited similar cohesion, Dopa peptoids were similar to 3 times more adhesive than Phe peptoids on mica. Compared with the peptides, Phe peptoid achieved only similar to 20% of Phe containing peptide adhesion, but the Dopa peptoids were >2-fold more adhesive than the Dopa peptides. Cation-pi interactions accounted for some but not all of the cohesive interactions. Our results were corroborated by molecular dynamics simulations and highlight the importance of backbone chemistry and the potential of peptoids or peptoid/peptide hybrids as wet adhesives and primers.
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