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Influence of water miscible organic solvents on alpha-chymotrypsin in solution and immobilized on Eupergit CM
Högskolan i Kalmar, Naturvetenskapliga institutionen.
Högskolan i Kalmar, Naturvetenskapliga institutionen.
Högskolan i Kalmar, Naturvetenskapliga institutionen.ORCID-id: 0000-0002-0407-6542
2006 (engelsk)Inngår i: Biotechnology letters, Vol. 28, nr 12, s. 929-935Artikkel i tidsskrift (Fagfellevurdert) Published
sted, utgiver, år, opplag, sider
2006. Vol. 28, nr 12, s. 929-935
HSV kategori
Forskningsprogram
Naturvetenskap, Organisk kemi
Identifikatorer
URN: urn:nbn:se:lnu:diva-739OAI: oai:DiVA.org:lnu-739DiVA, id: diva2:307477
Tilgjengelig fra: 2010-04-01 Laget: 2010-04-01 Sist oppdatert: 2015-04-16bibliografisk kontrollert
Inngår i avhandling
1. Towards novel applications for biomolecular interactions at surfaces
Åpne denne publikasjonen i ny fane eller vindu >>Towards novel applications for biomolecular interactions at surfaces
2013 (engelsk)Doktoravhandling, med artikler (Annet vitenskapelig)
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.

sted, utgiver, år, opplag, sider
Växjö: Linnaeus University Press, 2013
Serie
Linnaeus University Dissertations ; 149/2013
Emneord
molecular recognition, interactions, phage display, biomolecular interactions, phage, adenine, influenza virus replication, oseltamivir, imprinted polymers.
HSV kategori
Identifikatorer
urn:nbn:se:lnu:diva-29505 (URN)978-91-87427-53-4 (ISBN)
Disputas
2013-10-25, N2007, Västergård, Smålandsgatan 26E, Kalmar, 09:30 (engelsk)
Opponent
Tilgjengelig fra: 2013-10-08 Laget: 2013-10-08 Sist oppdatert: 2016-11-24bibliografisk kontrollert

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Olofsson, LinusSöderberg, PernillaNicholls, Ian Alan

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