Surface force measurements and simulations of mussel-derived peptide adhesives on wet organic surfaces
| Autor: | J. Herbert Waite, Michael V. Rapp, Zachary A. Levine, Chun Wu, Jacob N. Israelachvili, Jeetain Mittal, Gül H. Zerze, Ryan Gotchy Mullen, Joan-Emma Shea, Wei Wei |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
Chemical
Bioengineering Context (language use) 02 engineering and technology mussel foot proteins 010402 general chemistry 01 natural sciences Molecular dynamics symbols.namesake Models Adhesives protein folding Animals Organic chemistry Multidisciplinary Chemistry self-assembled monolayers Surface forces apparatus Self-assembled monolayer Adhesion molecular dynamics simulations Biological Sciences 021001 nanoscience & nanotechnology Bivalvia 0104 chemical sciences Models Chemical Chemical engineering Wettability symbols Adhesive Wetting van der Waals force Peptides 0210 nano-technology surface forces apparatus |
| Zdroj: | Levine, ZA; Rapp, MV; Wei, W; Mullen, RG; Wu, C; Zerze, GH; et al.(2016). Surface force measurements and simulations of mussel-derived peptide adhesives on wet organic surfaces. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 113(16), 4332-4337. doi: 10.1073/pnas.1603065113. UC Santa Barbara: Retrieved from: http://www.escholarship.org/uc/item/14z0q8qp Proceedings of the National Academy of Sciences of the United States of America, vol 113, iss 16 |
| DOI: | 10.1073/pnas.1603065113. |
| Popis: | Translating sticky biological molecules-such as mussel foot proteins (MFPs)-into synthetic, cost-effective underwater adhesives with adjustable nano- and macroscale characteristics requires an intimate understanding of the glue's molecular interactions. To help facilitate the next generation of aqueous adhesives, we performed a combination of surface forces apparatus (SFA) measurements and replica-exchange molecular dynamics (REMD) simulations on a synthetic, easy to prepare, Dopa-containing peptide (MFP-3s peptide), which adheres to organic surfaces just as effectively as its wild-type protein analog. Experiments and simulations both show significant differences in peptide adsorption on CH3-terminated (hydrophobic) and OH-terminated (hydrophilic) self-assembled monolayers (SAMs), where adsorption is strongest on hydrophobic SAMs because of orientationally specific interactions with Dopa. Additional umbrella-sampling simulations yield free-energy profiles that quantitatively agree with SFA measurements and are used to extract the adhesive properties of individual amino acids within the context of MFP-3s peptide adhesion, revealing a delicate balance between van der Waals, hydrophobic, and electrostatic forces. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|