Thiomer: Difference between revisions

Due to the binding of metal ions being essential for various enzymes to maintain their enzymatic activity, thiomers are potent reversible enzyme inhibitors. Many non-invasively administered drugs such as therapeutic peptides or nucleic acids are degraded on the mucosa by membrane bound enzymes strongly reducing their bioavailability. In case of oral administration this ‘enzymatic barrier’ is even more pronounced as an additional degradation caused by luminally secreted enzymes takes place. Because of their capability to bind zinc ions via thiol groups, thiomers are potent inhibitors of most membrane bound and secreted zinc-dependent enzymes. Due to this enzyme inhibitory effect, thiolated polymers can significantly improve the bioavailability of non-invasively administered drugs<ref>{{cite journal|last1=Valenta|first1=C|last2=Marschütz|first2=M|last3=Egyed|first3=C|last4=Bernkop-Schnürch|first4=A|title=Evaluation of the inhibition effect of thiolated poly(acrylates) on vaginal membrane bound aminopeptidase N and release of the model drug LH-RH|journal=J. Pharm. Pharmacol.|date=2002|volume=54|issue=5|pages=603–610|doi=10.1211/0022357021778907|pmid=12005354|s2cid=45367274|doi-access=free}}</ref><ref>{{cite journal|last1=Bernkop-Schnürch|first1=A|last2=Walker|first2=G|last3=Zarti|first3=H|title=Thiolation of polycarbophil enhances its inhibition of intestinal brush border membrane bound aminopeptidase N|journal=J. Pharm. Sci.|date=2001|volume=90|issue=11|pages=1907–1914|doi=10.1002/jps.1140|pmid=11745748}}</ref><ref>{{cite journal|last1=Bernkop-schnürch|first1=A|last2=Krauland|first2=AH|last3=Leitner|first3=VM|last4=Palmberger|first4=T|title=Thiomers: potential excipients for non-invasive peptide delivery systems|journal=Eur. J. Pharm. Biopharm.|date=2004|volume=58|issue=2|pages=253–263|doi=10.1016/j.ejpb.2004.03.032|pmid=15296953}}</ref>