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| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 03322naa a2200385 4500 | |
| 001 | oai:research.chalmers.se:d6ed043b-28c4-4da0-b3ef-148f7595b7a6 | |
| 003 | SwePub | |
| 008 | 171007s2010 | |||||||||||000 ||eng| | |
| 024 | 7 | a https://research.chalmers.se/publication/1292072 URI |
| 024 | 7 | a https://doi.org/10.1021/ac10164192 DOI |
| 040 | a (SwePub)cth | |
| 041 | a engb eng | |
| 042 | 9 SwePub | |
| 072 | 7 | a art2 swepub-publicationtype |
| 072 | 7 | a ref2 swepub-contenttype |
| 100 | 1 | a Nilebäck, Erik,d 1984u Chalmers tekniska högskola,Chalmers University of Technology4 aut0 (Swepub:cth)nileback |
| 245 | 1 0 | a Viscoelastic Sensing of Conformational Changes in Plasminogen Induced upon Binding of Low Molecular Weight Compounds |
| 264 | c 2010-09-20 | |
| 264 | 1 | b American Chemical Society (ACS),c 2010 |
| 520 | a Plasminogen is a precursor to the fibrinolytic enzyme plasmin and is known to undergo large conformational changes when subjected to low molecular lysine analogues such as tranexamic acid (TA) or epsilon-amino-n-caproic acid (EACA). Here, we demonstrate how well-controlled surface immobilization of biotinylated plasminogen allows for monitoring of the interaction between TA and EACA with plasminogen. The interaction was studied by the quartz crystal microbalance with dissipation monitoring (QCM-D) technique as well as by surface plasmon resonance (SPR) based sensing. QCM-D measures changes in acoustically coupled mass (by detection of changes in the resonance frequency of the crystal, Delta f) and is sensitive to changes in mass adsorbed on the sensor surface including how liquid medium is associated with this material. Through the dissipation factor (i.e., changes in the energy dissipation of the crystal oscillation, Delta D), QCM-D is also sensitive to the viscoelastic properties of material adsorbed to the sensor surface. Upon binding of TA or EACA, changes in the plasminogen structure were recorded as distinct, although small, Delta D responses which were used to determine affinity constants. By comparing native and truncated plasminogen, we conclude that the observed dissipation shifts were caused by conformational changes in the proteins leading to changes in the viscoelastic properties of the protein layer on the surface. These results demonstrate a novel application of the QCM-D technique, paving the way for a whole new approach to screening of this target for novel lead structures. | |
| 650 | 7 | a NATURVETENSKAPx Fysik0 (SwePub)1032 hsv//swe |
| 650 | 7 | a NATURAL SCIENCESx Physical Sciences0 (SwePub)1032 hsv//eng |
| 653 | a tranexamic acid | |
| 653 | a thickness | |
| 653 | a dna immobilization | |
| 653 | a film | |
| 653 | a subsequent hybridization | |
| 700 | 1 | a Westberg, F.u AstraZeneca AB4 aut |
| 700 | 1 | a Deinum, J.u AstraZeneca AB4 aut |
| 700 | 1 | a Svedhem, Sofia,d 1970u Chalmers tekniska högskola,Chalmers University of Technology4 aut0 (Swepub:cth)sofsv |
| 710 | 2 | a Chalmers tekniska högskolab AstraZeneca AB4 org |
| 773 | 0 | t Analytical Chemistryd : American Chemical Society (ACS)g 82:20, s. 8374-8376q 82:20<8374-8376x 0003-2700x 1520-6882 |
| 856 | 4 | u http://dx.doi.org/10.1021/ac1016419y FULLTEXT |
| 856 | 4 8 | u https://research.chalmers.se/publication/129207 |
| 856 | 4 8 | u https://doi.org/10.1021/ac1016419 |
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