Navigation überspringen
Universitätsbibliothek Heidelberg
Status: Bibliographieeintrag

Verfügbarkeit
Standort: ---
Exemplare: ---
heiBIB
 Online-Ressource
Verfasst von:Seehuber, Andrea [VerfasserIn]   i
 Dahint, Reiner [VerfasserIn]   i
Titel:Conformation and activity of glucose oxidase on homogeneously coated and nanostructured surfaces
Verf.angabe:A. Seehuber and R. Dahint
E-Jahr:2013
Jahr:May 17, 2013
Umfang:10 S.
Teil:volume:117
 year:2013
 number:23
 pages:6980-6989
 extent:10
Fussnoten:Gesehen am 12.08.2021
Titel Quelle:Enthalten in: The journal of physical chemistry <Washington, DC> / B
Ort Quelle:Washington, DC : Soc., 1997
Jahr Quelle:2013
Band/Heft Quelle:117(2013), 23, Seite 6980-6989
ISSN Quelle:1520-5207
Abstract:Protein unfolding and loss of protein function upon surface contact is a major problem in biotechnology and biomedicine. Using glucose oxidase (GOx) as a model protein, we investigated the impact of surface chemistry, topography, and confinement on enzyme activity, conformation, and affinity. A particular focus lay on the question whether the conformation of surface-bound proteins can be stabilized by embedding nanoscale adsorption sites, here in the form of monodisperse gold nanoparticles (AuNPs), into a protein-repelling matrix material. It was found that on homogeneous surfaces, GOx activity is generally lower than that in its native state and strongly affected by surface chemistry. Loss of activity is related to an increasing amount of β-sheets in the GOx secondary structure and a corresponding reduction of α-helical elements. In contrast, on AuNP surfaces, the effect of surface chemistry is negligible, and the amount of adsorbed protein only depends on particle size. The low activity of GOx on all nanostructures studied is again accompanied by an increase of β-sheet and a reduction of α-helical secondary structure. The major cause for protein unfolding on AuNPs thus seems to be the curvature of the surface. In addition, the data suggest that unfavorable orientation of the adsorbed enzyme also contributes to the loss of activity.
DOI:doi:10.1021/jp401906h
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Volltext: https://doi.org/10.1021/jp401906h
 DOI: https://doi.org/10.1021/jp401906h
Datenträger:Online-Ressource
Sprache:eng
K10plus-PPN:1766556752
Verknüpfungen:→ Zeitschrift

Permanenter Link auf diesen Titel (bookmarkfähig):  https://katalog.ub.uni-heidelberg.de/titel/68770225   QR-Code
zum Seitenanfang