Sökning: id:"swepub:oai:DiVA.org:kth-328852" > CaRA – A multi-purp...
Fältnamn | Indikatorer | Metadata |
---|---|---|
000 | 04133naa a2200481 4500 | |
001 | oai:DiVA.org:kth-328852 | |
003 | SwePub | |
008 | 230614s2022 | |||||||||||000 ||eng| | |
024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-3288522 URI |
024 | 7 | a https://doi.org/10.1016/j.nbt.2022.11.0052 DOI |
040 | a (SwePub)kth | |
041 | a engb eng | |
042 | 9 SwePub | |
072 | 7 | a ref2 swepub-contenttype |
072 | 7 | a art2 swepub-publicationtype |
100 | 1 | a Jönsson, Malinu KTH,Proteinvetenskap4 aut0 (Swepub:kth)u1ib7cr9 |
245 | 1 0 | a CaRA – A multi-purpose phage display library for selection of calcium-regulated affinity proteins |
264 | 1 | b Elsevier B.V.c 2022 |
338 | a print2 rdacarrier | |
500 | a QC 20230614 | |
520 | a Protein activity regulated by interactions with metal ions can be utilized for many different purposes, including biological therapies and bioprocessing, among others. Calcium ions are known to interact with the frequently occurring EF-hand motif, which can alter protein activity upon binding through an induced conformational change. The calcium-binding loop of the EF-hand motif has previously been introduced into a small protein domain derived from staphylococcal Protein A in a successful effort to render antibody binding dependent on calcium. Presented here, is a combinatorial library for calcium-regulated affinity, CaRA, based on this domain. CaRA is the first alternative scaffold library designed to achieve novel target specificities with metal-dependent binding. From this library, several calcium-dependent binders could be isolated through phage display campaigns towards a set of unrelated target proteins (IgE Cε3-Cε4, TNFα, IL23, scFv, tPA, PCSK9 and HER3) useful for distinct applications. Overall, these monomeric CaRA variants showed high stability and target affinities within the nanomolar range. They displayed considerably higher melting temperatures in the presence of 1 mM calcium compared to without calcium. Further, all discovered binders proved to be calcium-dependent, with the great majority showing complete lack of target binding in the absence of calcium. As demonstrated, the CaRA library is highly capable of providing protein-binding domains with calcium-dependent behavior, independent of the type of target protein. These binding domains could subsequently be of great use in gentle protein purification or as novel therapeutic modalities. | |
650 | 7 | a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe |
650 | 7 | a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng |
653 | a Calcium-dependent binding | |
653 | a Phage display selection | |
653 | a Protein engineering | |
653 | a Z-domain | |
700 | 1 | a Scheffel, Juliau KTH,Proteinteknologi4 aut0 (Swepub:kth)u1y97f4h |
700 | 1 | a Larsson, Emmau KTH,Proteinvetenskap4 aut0 (Swepub:kth)u1bqcxhc |
700 | 1 | a Möller, Maritu KTH,Proteinvetenskap4 aut0 (Swepub:kth)u1ht1lyx |
700 | 1 | a Rossi, Gabriellau KTH,Proteinvetenskap4 aut0 (Swepub:kth)u1cn7jy9 |
700 | 1 | a Lundqvist, Magnusu KTH,Proteinteknologi4 aut0 (Swepub:kth)u1hfekeg |
700 | 1 | a Rockberg, Johanu KTH,Proteinvetenskap4 aut0 (Swepub:kth)u130jo0a |
700 | 1 | a Uhlén, Mathiasu KTH,Proteinvetenskap,Department of Protein Science, KTH-Royal Institute of Technology, SE-10691, Stockholm, Sweden4 aut0 (Swepub:kth)u1dulvmw |
700 | 1 | a Tegel, Hannau KTH,Proteinvetenskap4 aut0 (Swepub:kth)u1nou8yx |
700 | 1 | a Kanje, Sara,d 1986-u KTH,Proteinvetenskap4 aut0 (Swepub:kth)u1t204cn |
700 | 1 | a Hober, Sophia,c Professor,d 1965-u KTH,Proteinvetenskap4 aut0 (Swepub:kth)u11qqzc1 |
710 | 2 | a KTHb Proteinvetenskap4 org |
773 | 0 | t New Biotechnologyd : Elsevier B.V.g 72, s. 159-167q 72<159-167x 1871-6784x 1876-4347 |
856 | 4 | u https://doi.org/10.1016/j.nbt.2022.11.005y Fulltext |
856 | 4 | u https://api.elsevier.com/content/abstract/scopus_id/85142821413 |
856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-328852 |
856 | 4 8 | u https://doi.org/10.1016/j.nbt.2022.11.005 |
Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.