id:"swepub:oai:DiVA.org:kth-10016"
Sökning: id:"swepub:oai:DiVA.org:kth-10016" > Engineering of a fe...
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| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 03196naa a2200397 4500 | |
| 001 | oai:DiVA.org:kth-10016 | |
| 003 | SwePub | |
| 008 | 090304s2008 | |||||||||||000 ||eng| | |
| 024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-100162 URI |
| 024 | 7 | a https://doi.org/10.1093/protein/gzn0282 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 Jonsson, Andreas,d 1974-u KTH,Molekylär Bioteknologi,Biotherapy and Bacterial Display4 aut0 (Swepub:kth)u1rkd9ig |
| 245 | 1 0 | a Engineering of a femtomolar affinity binding protein to human serum albumin |
| 264 | c 2008-05-13 | |
| 264 | 1 | b Oxford University Press (OUP),c 2008 |
| 338 | a print2 rdacarrier | |
| 500 | a QC 20100722 | |
| 520 | a We describe the development of a novel serum albumin binding protein showing an extremely high affinity (K(D)) for HSA in the femtomolar range. Using a naturally occurring 46-residue three-helix bundle albumin binding domain (ABD) of nanomolar affinity for HSA as template, 15 residues were targeted for a combinatorial protein engineering strategy to identify variants showing improved HSA affinities. Sequencing of 55 unique phage display-selected clones showed a strong bias for wild-type residues at nine positions, whereas various changes were observed at other positions, including charge shifts. Additionally, a few non-designed substitutions appeared. On the basis of the sequences of 12 variants showing high overall binding affinities and slow dissociation rate kinetics, a set of seven 'second generation' variants were constructed. One variant denoted ABD035 displaying wild-type-like secondary structure content and excellent thermal denaturation/renaturation properties showed an apparent affinity for HSA in the range of 50-500 fM, corresponding to several orders of magnitude improvement compared with the wild-type domain. The ABD035 variant also showed an improved affinity toward serum albumin from a number of other species, and a capture experiment involving human serum indicated that the selectivity for serum albumin had not been compromised from the affinity engineering. | |
| 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 affinity/combinatorial protein engineering | |
| 653 | a Molecular biology | |
| 653 | a Molekylärbiologi | |
| 700 | 1 | a Dogan, Jakobu KTH,Molekylär Bioteknologi4 aut0 (Swepub:kth)u1xpotzq |
| 700 | 1 | a Harne, Nina4 aut |
| 700 | 1 | a Abrahmsén, Lars4 aut |
| 700 | 1 | a Nygren, Per-Åkeu KTH,Molekylär Bioteknologi4 aut0 (Swepub:kth)u1zhverl |
| 710 | 2 | a KTHb Molekylär Bioteknologi4 org |
| 773 | 0 | t Protein Engineering Design & Selectiond : Oxford University Press (OUP)g 21:8, s. 515-527q 21:8<515-527x 1741-0126x 1741-0134 |
| 856 | 4 | u https://academic.oup.com/peds/article-pdf/21/8/515/4386754/gzn028.pdf |
| 856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-10016 |
| 856 | 4 8 | u https://doi.org/10.1093/protein/gzn028 |
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