Ferrari, Enrico and Soloviev, Mikhail and Niranjan, Dhevahi and Arsenault, Jason and Gu, Chunjing and Vallis, Yvonne and O’Brien, John and Davletov, Bazbek (2012) Assembly of protein building blocks using a short synthetic peptide. Bioconjugate Chemistry, 23 (3). pp. 479-484. ISSN 1043-1802
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Full text URL: http://dx.doi.org/10.1021/bc2005208
Combining proteins or their defined domains offers new enhanced functions. Conventionally, two proteins are either fused into a single polypeptide chain by recombinant means or chemically cross-linked. However, these strategies can have drawbacks such as poor expression (recombinant fusions) or aggregation and inactivation (chemical cross-linking), especially in the case of large multifunctional proteins. We developed a new linking method which allows site-oriented, noncovalent, yet irreversible stapling of modified proteins at neutral pH and ambient temperature. This method is based on two distinct polypeptide linkers which self-assemble in the presence of a specific peptide staple allowing on-demand and irreversible combination of protein domains. Here we show that linkers can either be expressed or be chemically conjugated to proteins of interest, depending on the source of the proteins. We also show that the peptide staple can be shortened to 24 amino acids still permitting an irreversible combination of functional proteins. The versatility of this modular technique is demonstrated by stapling a variety of proteins either in solution or to surfaces.
|Subjects:||C Biological Sciences > C720 Biological Chemistry|
C Biological Sciences > C700 Molecular Biology, Biophysics and Biochemistry
|Divisions:||College of Science > School of Life Sciences|
|Deposited By:||Enrico Ferrari|
|Deposited On:||15 Oct 2012 20:44|
|Last Modified:||29 Nov 2013 10:10|
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