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111In-labeled NOTA-conjugated Affibody molecules for visualization of HER3 expression in malignant tumors
KTH, Skolan för bioteknologi (BIO), Proteinteknologi.
Vise andre og tillknytning
2014 (engelsk)Inngår i: European Journal of Nuclear Medicine and Molecular Imaging, ISSN 1619-7070, E-ISSN 1619-7089, Vol. 41, s. S311-S311Artikkel i tidsskrift, Meeting abstract (Annet vitenskapelig) Published
sted, utgiver, år, opplag, sider
2014. Vol. 41, s. S311-S311
HSV kategori
Identifikatorer
URN: urn:nbn:se:kth:diva-161572ISI: 000348841900497OAI: oai:DiVA.org:kth-161572DiVA, id: diva2:798303
Konferanse
Annual Congress of the European-Association-of-Nuclear-Medicine (EANM), OCT 18-22, 2014, Gothenburg, SWEDEN
Merknad

QC 20150326

Tilgjengelig fra: 2015-03-26 Laget: 2015-03-13 Sist oppdatert: 2017-12-04bibliografisk kontrollert
Inngår i avhandling
1. Combinatorial Protein Engineering Of Affibody Molecules Using E. Coli Display And Rational Design Of Affibody-Based Tracers For Medical Imaging
Åpne denne publikasjonen i ny fane eller vindu >>Combinatorial Protein Engineering Of Affibody Molecules Using E. Coli Display And Rational Design Of Affibody-Based Tracers For Medical Imaging
2017 (engelsk)Doktoravhandling, med artikler (Annet vitenskapelig)
Abstract [en]

Directed evolution is today an established strategy for generation of new affinity proteins. This thesis describes the development of a cell-display method using Escherichia coli for directed evolution of Affibody molecules. Further, the thesis describes rational design of Affibody-based tracers, intended for future patient stratification using medical imaging. Fusing recombinant proteins to various autotransporters is a promising approach for efficient surface display on the surface of E. coli, as well as for construction of high-complexity libraries. In paper I, we successfully engineered an expression vector for display of Affibody molecules using the autotransporter AIDA-I. In paper II, a large Affibody library of 2.3x109 variants was constructed and screening using FACS resulted in new specific binders in the nanomolar range. In paper III, we demonstrated Sortase-mediated secretion and conjugation of binders directly from the E. coli surface. 

The three following studies describe rational design of Affibody-based tracers against two cancer-associated targets for molecular imaging. First, anti-HER3 Affibody molecules were labelled with 111In, and SPECT imaging showed that the conjugates specifically targeted HER3-expressing xenografts. Furthermore, labeling with 68Ga for PET imaging showed that tumor uptake correlated with HER3 expression, suggesting that the tracers have potential for patient stratification. The last study describes the development and investigation of anti-EGFR Affibody-based imaging agents. Labeled with 89Zr, the Affibody tracer demonstrated higher tumor uptake at 3 h post injection than the anti-EGFR antibody cetuximab at 48 h post injection. 

In conclusion, this thesis describes new tools and knowledge that will hopefully contribute to the development of affinity proteins for biotechnology, therapy and medical imaging in the future. 

 

sted, utgiver, år, opplag, sider
Stockholm: KTH Royal Institute of Technology, 2017. s. 80
Serie
TRITA-BIO-Report, ISSN 1654-2312 ; 2017:17
Emneord
directed evolution, microbial display, E. coli, Affibody molecule, autotransporter, medical imaging, HER receptor family, Sortase A
HSV kategori
Forskningsprogram
Bioteknologi
Identifikatorer
urn:nbn:se:kth:diva-213451 (URN)978-91-7729-504-4 (ISBN)
Disputas
2017-10-06, F3, Lindstedtsvägen 26, Sing-Sing, floor 2, KTH Campus, Stockholm, 13:00 (engelsk)
Opponent
Veileder
Merknad

QC 20170904

Tilgjengelig fra: 2017-09-05 Laget: 2017-08-31 Sist oppdatert: 2017-09-05bibliografisk kontrollert

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Löfblom, JohnStåhl, Stefan

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Andersson, Ken G.Malm, M.Sandström, M.Löfblom, JohnStåhl, Stefan
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