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The albumin-binding domain as a scaffold for protein engineering
KTH, School of Biotechnology (BIO), Protein Technology.ORCID iD: 0000-0002-6104-6446
KTH, School of Biotechnology (BIO), Protein Technology.ORCID iD: 0000-0003-0605-8417
2013 (English)In: Computational and Structural Biotechnology Journal, ISSN 2001-0370, Vol. 6, no 7, a5- p.Article in journal (Refereed) Published
Abstract [en]

The albumin-binding domain is a small, three-helical protein domain found in various surface proteins expressed by gram-positive bacteria. Albumin binding is important in bacterial pathogenesis and several homologous domains have been identified. Such albumin-binding regions have been used for protein purification or immobilization. Moreover, improvement of the pharmacokinetics, through the non-covalent association to albumin, by fusing such domains to therapeutic proteins has been shown to be successful. Domains derived from streptococcal protein G and protein PAB from Finegoldia magna, which share a common origin and therefore represent an interesting evolutionary system, have been thoroughly studied structurally and functionally. Their albumin-binding sites have been mapped and these domains form the basis for a wide range of protein engineering approaches. By substitution-mutagenesis they have been engineered to achieve a broader specificity, an increased stability or an improved binding affinity, respectively. Furthermore, novel binding sites have been incorporated either by replacing the original albumin-binding surface, or by complementing it with a novel interaction interface. Combinatorial protein libraries, where several residues have been randomized simultaneously, have generated a large number of new variants with desired binding characteristics. The albuminbinding domain has also been utilized to explore the relationship between three-dimensional structure and amino acid sequence. Proteins with latent structural information built into their sequence, where a single amino acid substitution shifts the equilibrium in favor of a different fold with a new function, have been designed. Altogether, these examples illustrate the versatility of the albumin-binding domain as a scaffold for protein engineering.

Place, publisher, year, edition, pages
2013. Vol. 6, no 7, a5- p.
Keyword [en]
Affinity maturation, Affinity protein, Albumin, Bispecific, Protein domain, Specificity
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:kth:diva-150870DOI: 10.5936/csbj.201303009Scopus ID: 2-s2.0-84902175200OAI: oai:DiVA.org:kth-150870DiVA: diva2:745805
Note

QC 20140911

Available from: 2014-09-11 Created: 2014-09-11 Last updated: 2014-09-11Bibliographically approved

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Nilvebrant, JohanHober, Sophia

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