• English
    • Norsk
  • English 
    • English
    • Norsk
  • Administration
View Item 
  •   Home
  • Øvrige samlinger
  • Høstingsarkiver
  • CRIStin høstingsarkiv
  • View Item
  •   Home
  • Øvrige samlinger
  • Høstingsarkiver
  • CRIStin høstingsarkiv
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

Studies of dynamic binding of amino acids to TiO2 nanoparticle surfaces by Solution NMR and Molecular Dynamics Simulations

mengjun, xue; Sampath, Janani; Gebart, Rachel; Haugen, Håvard Jostein; Lyngstadaas, Ståle Petter; Pfaendtner, Jim; Drobny, Gary
Journal article; AcceptedVersion; Peer reviewed
View/Open
Drobny_paper.pdf (819.7Kb)
Year
2020
Permanent link
http://urn.nb.no/URN:NBN:no-81521

CRIStin
1820500

Metadata
Show metadata
Appears in the following Collection
  • Det odontologiske fakultet [1240]
  • CRIStin høstingsarkiv [22570]
Original version
Langmuir. 2020:acs.langmuir.0c01256, DOI: https://doi.org/10.1021/acs.langmuir.0c01256
Abstract
Adsorption of biomolecules onto material surfaces involves a potentially complex mechanism where molecular species interact to varying degrees with a heterogeneous material surface. Surface adsorption studies by atomic force microscopy (AFM), Sum Frequency Generation (SFG) spectroscopy, and solid state NMR (ssNMR), detect the structures and interactions of biomolecular species that are bound to material surfaces and which, in the absence of a solid liquid interface, do not exchange rapidly between surface-bound forms and free molecular species in bulk solution. Solution NMR has the potential to complement these techniques by detecting and studying transiently bound biomolecules at the liquid-solid interface. Herein we show that dark-state exchange saturation transfer (DEST) NMR experiments on gel-stabilized TiO2 nanoparticle (NP) samples detect several forms of biomolecular adsorption onto titanium (IV) oxide surfaces. Specifically, we use the DEST approach to study the interaction of amino acids arginine (Arg), lysine (Lys), leucine (Leu), alanine (Ala), and aspartic acid (Asp) with TiO2 rutile nanoparticle surfaces. Whereas Leu, Ala, and Asp display only a single weakly interacting form in the presence of TiO2 nanoparticles , Arg and Lys displayed at least two distinct bound forms: a species that is surface bound and retains a degree of reorientational motion, and a second more tightly bound form characterized by broadened DEST profiles upon addition of TiO2 nanoparticles. Molecular Dynamics simulations indicate different surface bound states for both Lys and Arg depending on the degree of TiO2 surface hydroxylation, but only a single bound state for Asp regardless of the degree of surface hydroxylation, in agreement with results obtained from analysis of DEST profiles.
 
Responsible for this website 
University of Oslo Library


Contact Us 
duo-hjelp@ub.uio.no


Privacy policy
 

 

For students / employeesSubmit master thesisAccess to restricted material

Browse

All of DUOCommunities & CollectionsBy Issue DateAuthorsTitlesThis CollectionBy Issue DateAuthorsTitles

For library staff

Login
RSS Feeds
 
Responsible for this website 
University of Oslo Library


Contact Us 
duo-hjelp@ub.uio.no


Privacy policy