AVS 59th Annual International Symposium and Exhibition | |
Biomaterial Interfaces | Wednesday Sessions |
Session BI+SS+NS-WeM |
Session: | Bio/Nano Interfaces with Applications in Biomedicine and Energy |
Presenter: | M. Valtiner, Max-Planck-Institut fur Eisenforschung, Germany |
Authors: | M. Valtiner, Max-Planck-Institut fur Eisenforschung, Germany S.H. Donaldson, University of California, Santa Barbara M.A. Gebbie, University of California, Santa Barbara J.N. Israelachvili, University of California, Santa Barbara |
Correspondent: | Click to Email |
A molecular-level understanding of interaction forces and dynamics between asymmetric apposing surfaces plays a key-role in utilizing molecular structures for functional surfaces in biological and materials applications. To quantify interaction forces and binding dynamics between apposing surfaces in terms of their molecular architecture we developed a novel surface-forces-apparatus experiment, using self-assembled monolayers (SAMs) on atomically-smooth gold. Varying the SAM head-group allowed to quantitatively identify and control which interaction forces dominated between the SAM surfaces and surfaces coated with short-chain, end-functionalized polyethylene-glycol (PEG) polymers extending from lipid-bilayers [1].
Three different SAM-terminations were studied: (a) carboxylic-acid, (b) alcohol, and (c) methyl head-group terminations. These functionalities allowed for the quantification of (a) specific acid-base bindings, (b) steric effects of PEG chains, and (c) adhesion of hydrophobic segments of the polymer-backbone, all as function of the solution pH. The pH-dependent acid-base binding appears to be a specific, charge-mediated hydrogen bond between oppositely-charged carboxylic-acid and amine functionalities, above the acid-pKA and below the amine-pKA. The long-range electrostatic “steering” of acid-base pairs leads to high binding probability even at distances close-to-full-extension of the PEG tethers, a result which has potentially important implications for protein-folding, enzymatic catalysis and biomaterial development.
[1] M. Valtiner et al., JACS, 2012, 1746