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Monitoring of influenza virus hemagglutinin in process samples using weak affinity ligands and surface plasmon resonance
Linköpings universitet, Institutionen för fysik, kemi och biologi, Teknisk biologi. Linköpings universitet, Tekniska högskolan.ORCID-id: 0000-0001-9711-794X
Linköpings universitet, Institutionen för fysik, kemi och biologi. Linköpings universitet, Tekniska högskolan.
School of Pure and Applied Natural Sciences, University of Kalmar, SE-391 82 Kalmar, Sweden.
Linköpings universitet, Institutionen för fysik, kemi och biologi. Linköpings universitet, Tekniska högskolan.
Vise andre og tillknytning
2008 (engelsk)Inngår i: Analytica Chimica Acta, ISSN 0003-2670, E-ISSN 1873-4324, Vol. 623, s. 66-75Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Surface plasmon resonance (SPR) was used to screen the interaction between a variety of affinity ligands and hemagglutinin (HA) from human influenza virus, with the aim of identifying low affinity ligands useful for the development of a rapid bioanalytical sensor. Three sialic acid-based structures and four lectins were evaluated as sensor ligands. The sialic acid-based ligands included a natural sialic acid-containing glycoprotein, human α1-acid glycoprotein (α1-AGP), and two synthetic 6′-sialyllactose-conjugates, with varying degree of substitution. The interaction of HA with the four lectin-based ligands, concanavalin A (Con A), wheat germ agglutinin (WGA), Maackia amurensis lectin (MAL), and Sambucus nigra agglutinin (SNA), showed a wide variation of affinity strengths. Affinity and kinetics data were estimated. Strong affinities were observed for Con A, WGA, α1-AGP, and a 6′-sialyllactose-conjugate with a high substitution degree, and low affinities were observed for MAL and a 6′-sialyllactose-conjugate with low substitution.

The main objective, to identify a low affinity ligand which could be used for on-line monitoring and product quantification, was met by a 6′-sialyllactose–ovalbumin conjugate that had 0.6 mol ligand per mol carrier protein. The apparent affinity of this ligand was estimated to be 1.5 ± 0.03 μM (KD) on the SPR surface. Vaccine process samples containing HA were analyzed in the range 10–100 μg HA mL−1 and correlated with single-radial immunodiffusion. The coefficient of variation on the same chip was between 0.010 and 0.091.

sted, utgiver, år, opplag, sider
Elsevier, 2008. Vol. 623, s. 66-75
Emneord [en]
Influenza virus hemagglutinin; Affinity ligand; Surface plasmon resonance; Low affinity; Weak affinity
HSV kategori
Identifikatorer
URN: urn:nbn:se:liu:diva-44210DOI: 10.1016/j.aca.2008.06.005Lokal ID: 76040OAI: oai:DiVA.org:liu-44210DiVA, id: diva2:265071
Tilgjengelig fra: 2009-10-10 Laget: 2009-10-10 Sist oppdatert: 2019-01-22bibliografisk kontrollert
Inngår i avhandling
1. Exploring the SPR methodology for monitoring of critical attributes in toxicity testing and bioproduction
Åpne denne publikasjonen i ny fane eller vindu >>Exploring the SPR methodology for monitoring of critical attributes in toxicity testing and bioproduction
2012 (engelsk)Licentiatavhandling, med artikler (Annet vitenskapelig)
Abstract [en]

Analysis of biological components is central in bioprocess monitoring, process control, product quality control and cell based toxicity assaying. One of these themes that is pursued in this thesis is the use of biosensors for monitoring of molecular markers, exploiting the natural selectivity of biomolecules. Another is the use of glycoconjugates to monitor the activity of biomolecules in a flu vaccine process is studied and were the sensor is based on the concept of weak affinity giving fast response time for the sensor.

A third theme is monitoring of cell cultures used for toxicity testing different protein markers is of interest.

When developing biosensor surfaces for new antigens commercial preparations of antibodies are often used. In this work we have chosen to look at lactate dehydrogenase (LDH) and describe the preparation and characterisation of antibody used in biosensor surface development.

The design of a sensor surface is important for the characteristics of a sensor. By binding antibodies in an oriented manner to the surface a better control of the properties of the antibodies is achieved. The demonstrated method also has the advantage of in situ purification and provides a flexible platform for antibody evaluation and sensor development.

In one sentence this thesis explores the possibility of utilizing recognition elements of a biosensor surface. In particular, surface plasmon resonance (SPR) is used as the primary biosensing tool, however most findings in are relevant for other biosensors.

Moreover, the thesis approaches existing bioanalytical impediments, such as purity and accessibility of the recognition elements on the sensor surface and preparation strategies to achieve this.

sted, utgiver, år, opplag, sider
Linköping: Linköping University Electronic Press, 2012. s. 19
Serie
Linköping Studies in Science and Technology. Thesis, ISSN 0280-7971 ; 1517
HSV kategori
Identifikatorer
urn:nbn:se:liu:diva-73410 (URN)LIU-TEK-LIC-2012:2 (Lokal ID)978-91-7519-971-9 (ISBN)LIU-TEK-LIC-2012:2 (Arkivnummer)LIU-TEK-LIC-2012:2 (OAI)
Presentation
2012-01-31, Panck, Fysikhuset, Campus Valla, Linköpings Universitet, Linköping, 09:15 (svensk)
Opponent
Veileder
Tilgjengelig fra: 2012-01-03 Laget: 2012-01-03 Sist oppdatert: 2019-01-22bibliografisk kontrollert

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