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Stability towards a...
Stability towards alkaline conditions can be engineered into a protein ligand
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Gulich, S. (författare)
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Linhult, M. (författare)
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- Nygren, Per-Åke (författare)
- KTH,Bioteknologi
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- Uhlén, Mathias (författare)
- KTH,Bioteknologi
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- Hober, Sophia (författare)
- KTH,Bioteknologi
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(creator_code:org_t)
- 2000
- 2000
- Engelska.
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Ingår i: Journal of Biotechnology. - 0168-1656 .- 1873-4863. ; 80:2, s. 169-178
- Relaterad länk:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- One of the problems with a proteinaceous affinity ligand is their sensitivity to alkaline conditions. Here, we show that a simple and straightforward strategy consisting of replacing all asparagine residues with other amino acids can dramatically improve the chemical stability of a protein towards alkaline conditions. As a model, a Streptococcal albumin-binding domain (ABD) was used. The engineered variant showed higher stability towards 0.5 M NaOH, as well as higher thermal stability compared to its native counterpart. This protein engineering approach could potentially also be used for other protein ligands to eliminate the sensitivity to alkaline cleaning-in-place (CIP) conditions.
Nyckelord
- albumin-binding domain
- cleaning-in-place
- deamidation
- human serum albumin
- protein engineering
- serum albumin
- deamidation
- residues
- asparaginyl
- peptides
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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