Applications of aliphatic unsaturated non-proteinogenic α-H-α-amino acids

Rutjes, Floris P. J. T.; Wolf, Larissa B.; Schoemaker, Hans E.

doi:10.1039/b001538p

Cited by 78 publications

(23 citation statements)

References 96 publications

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“…The chemical versatility of amino acids containing unsaturated side chains has recently been reviewed. 56 Furthermore, incorporation of halides, especially fluoride, can have dramatic effects on the physical properties of materials. Extension of the set of amino acid building blocks to unnatural analogues that can be utilized by the protein production mechanism of living systems would therefore enlarge the possibilities of proteinbased materials.…”

Section: Increasing the Scope Of Protein Engineeringmentioning

confidence: 99%

Protein-based materials, toward a new level of structural control

2001

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Through billions of years of evolution nature has created and refined structural proteins for a wide variety of specific purposes. Amino acid sequences and their associated folding patterns combine to create elastic, rigid or tough materials. In many respects, nature's intricately designed products provide challenging examples for materials scientists, but translation of natural structural concepts into bio-inspired materials requires a level of control of macromolecular architecture far higher than that afforded by conventional polymerization processes. An increasingly important approach to this problem has been to use biological systems for production of materials. Through protein engineering, artificial genes can be developed that encode protein-based materials with desired features. Structural elements found in nature, such as b-sheets and a-helices, can be combined with great flexibility, and can be outfitted with functional elements such as cell binding sites or enzymatic domains. The possibility of incorporating non-natural amino acids increases the versatility of protein engineering still

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Section: Increasing the Scope Of Protein Engineeringmentioning

confidence: 99%

Protein-based materials, toward a new level of structural control

2001

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“…Applications include selective tagging of proteins with probes and protein engineering for structure͞ function analysis (11,12). Already the method has permitted the incorporation of a diverse set of methionine analogs with alkyl and unsaturated side chains (13,14), the latter suggesting opportunities for subsequent chemical reaction (15)(16)(17).…”

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Incorporation of azides into recombinant proteins for chemoselective modification by the Staudinger ligation

Kiick

Saxon

Tirrell

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

883

754

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The introduction of chemically unique groups into proteins by means of non-natural amino acids has numerous applications in protein engineering and functional studies. One method to achieve this involves the utilization of a non-natural amino acid by the cell's native translational apparatus. Here we demonstrate that a methionine surrogate, azidohomoalanine, is activated by the methionyl-tRNA synthetase of Escherichia coli and replaces methionine in proteins expressed in methionine-depleted bacterial cultures. We further show that proteins containing azidohomoalanine can be selectively modified in the presence of other cellular proteins by means of Staudinger ligation with triarylphosphine reagents. Incorporation of azide-functionalized amino acids into proteins in vivo provides opportunities for protein modification under native conditions and selective labeling of proteins in the intracellular environment.

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“…A wide variety of side-chains can be introduced through the use of chain extension reactions, such as metathesis and cross coupling reactions [39,40]. The Suzuki reaction has proven useful for the latter, although the amino acid does need to be protected (Scheme 12.11) [41], and sometimes the protected amino alcohol, rather than acid, has been employed [42][43][44].…”

Section: Modifications Of the Side-chainmentioning

confidence: 99%

Synthesis of Unnatural/Nonproteinogenic α‐Amino Acids

Ager¹

2009

Amino Acids, Peptides and Proteins in Organic Chemistry

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Applications of aliphatic unsaturated non-proteinogenic α-H-α-amino acids

Cited by 78 publications

References 96 publications

Protein-based materials, toward a new level of structural control

Protein-based materials, toward a new level of structural control

Incorporation of azides into recombinant proteins for chemoselective modification by the Staudinger ligation

Synthesis of Unnatural/Nonproteinogenic α‐Amino Acids

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