The effect of delmopinol on glucosyltransferase adsorbed on to saliva-coated hydroxyapatite

D. Steinberg*, D. Beeman, W. H. Bowen

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

34 Scopus citations

Abstract

The aim was to explore the effects of delmopinol, a substituted amino-alcohol compound recently reported as a potential antiplaque agent, on GTF activity in solution and when adsorbed on to sHA. Delmopinol was without a significant effect on GTF activity in solution. In contrast, a reduction in the bound glucans synthesized by the adsorbed GTF was found in the presence of delmopinol. Delmopinol did not displace the adsorbed GTF from the sHA, nor was there significant desorption of glucans from sHA. The total glucan synthesis (bound and unbound) was reduced in the presence of delmopinol. Inhibition of GTF was not reversed by sucrose. Inhibition of GTF activity by delmopinol apparently results from drug-enzyme interaction on the surface of sHA beads. These observations provide further support for the important differences in the properties of adsorbed GTF and GTF in solution, illustrating that GTF-drug interaction differs between enzyme adsorbed to surfaces and enzyme in solution.

Original languageAmerican English
Pages (from-to)33-38
Number of pages6
JournalArchives of Oral Biology
Volume37
Issue number1
DOIs
StatePublished - Jan 1992
Externally publishedYes

Bibliographical note

Funding Information:
USPHS DE 07907f rom the National Instituteo f Dental Research,N IH, Bethesda,M D; Fogarty Fellowship FOS TWO4389a nd the Fulbright ResearcheAr ward.

Keywords

  • adhesion
  • adsorbed glucosyltransferase
  • delmopinol
  • saliva-coated hydroxyapatite
  • soluble glucosyltransferase

Fingerprint

Dive into the research topics of 'The effect of delmopinol on glucosyltransferase adsorbed on to saliva-coated hydroxyapatite'. Together they form a unique fingerprint.

Cite this