Öppna denna publikation i ny flik eller fönster >>2013 (Engelska)Doktorsavhandling, sammanläggning (Övrigt vetenskapligt)
Abstract [en]
The focus of this thesis has been to examine two new concepts involving the interaction of biological agents with synthetic material surfaces.
The feasibility of deploying phage display techniques for the screening of materials in non-biological media was examined in two studies. Firstly, the utility of a phage library based on the M13 phage was used to identify peptides with affinity for α-chymotrypsin in media containing significant amounts of an organic solvent, acetonitrile. The selected peptides were demonstrated to inhibit enzyme autolysis. The influence of immobilization to the substrate used in the screening studies, Eupergit®, on the function of this enzyme in organic solvents was examined; enhanced enzyme resilience to organic solvents was demonstrated. Secondly, phage display screening for cyclic heptapeptide motifs selective for adenine was undertaken using an adenine derivatized glass surfaces as a target. A peptide with affinity for adenine was identified and quartz crystal microbalance studies demonstrated selectivity for the adeninyl moiety.
Finally, the influence of oseltamivir molecularly imprinted polymer particles on the capacity of avian influenza A virus H1N1 to replicate in Madin-Darby Canine Kidney cells was investigated. The polymer matrix was shown to demonstrate a general though small suppression of virus replication.
Ort, förlag, år, upplaga, sidor
Växjö: Linnaeus University Press, 2013
Serie
Linnaeus University Dissertations ; 149/2013
Nyckelord
molecular recognition, interactions, phage display, biomolecular interactions, phage, adenine, influenza virus replication, oseltamivir, imprinted polymers.
Nationell ämneskategori
Biomaterialvetenskap
Identifikatorer
urn:nbn:se:lnu:diva-29505 (URN)978-91-87427-53-4 (ISBN)
Disputation
2013-10-25, N2007, Västergård, Smålandsgatan 26E, Kalmar, 09:30 (Engelska)
Opponent
2013-10-082013-10-082016-11-24Bibliografiskt granskad