Structural Modification of a Periodic Polypeptide through Biosynthetic Replacement of Proline with Azetidine-2-carboxylic Acid

Repetitive polypeptides comprising 16 repeats of the sequence −(AlaGly)3ProGluGly− (1a) have been prepared from Escherichia coli as overexpressed recombinant proteins. Partial in vivo replacement of the proline (Pro) residues in sequence 1a with l-azetidine-2-carboxylic acid (Aze) was achieved by ex...

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Bibliographic Details
Published in:Macromolecules 1996-02, Vol.29 (5), p.1442-1444
Main Authors: Deming, Timothy J, Fournier, Maurille J, Mason, Thomas L, Tirrell, David A
Format: Article
Language:English
Subjects:
Aminoacid polymers
Applied sciences
Biological and medical sciences
Biotechnology
Exact sciences and technology
Fundamental and applied biological sciences. Psychology
Genetic engineering
Genetic technics
Methods. Procedures. Technologies
Modification of gene expression level
Physicochemistry of polymers
Synthetic biopolymers
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Summary:Repetitive polypeptides comprising 16 repeats of the sequence −(AlaGly)3ProGluGly− (1a) have been prepared from Escherichia coli as overexpressed recombinant proteins. Partial in vivo replacement of the proline (Pro) residues in sequence 1a with l-azetidine-2-carboxylic acid (Aze) was achieved by expression of the target protein in medium containing Aze and lacking Pro. NMR and amino acid analysis for residual proline in the polymer indicated 25−40% replacement of Pro by Aze. While polymers of 1a form conformationally disordered solids, incorporation of Aze allows this material to adopt a β-sheet structure in the solid state.
ISSN:0024-9297
1520-5835
DOI:10.1021/ma9510698