scholarly journals Side-chain-to-tail cyclization of ribosomally derived peptides promoted by aryl and alkyl amino-functionalized unnatural amino acids

2016 ◽  
Vol 14 (24) ◽  
pp. 5803-5812 ◽  
Author(s):  
John R. Frost ◽  
Zhijie Wu ◽  
Yick Chong Lam ◽  
Andrew E. Owens ◽  
Rudi Fasan
Keyword(s):  
Amino Acids ◽  
Unnatural Amino Acids ◽  
Cyclic Peptides ◽  
Side Chain

A strategy for the production of side-chain-to-tail cyclic peptides from ribosomally derived polypeptide precursors is reported.

Molecular Design and Synthesis of Artificial Ion Channels Based on Cyclic Peptides Containing Unnatural Amino Acids

2001 ◽  
Vol 66 (9) ◽  
pp. 2978-2989 ◽  
Author(s):  
Hitoshi Ishida ◽  
Zhi Qi ◽  
Masahiro Sokabe ◽  
Kiyoshi Donowaki ◽  
Yoshihisa Inoue
Keyword(s):  
Amino Acids ◽  
Ion Channels ◽  
Unnatural Amino Acids ◽  
Cyclic Peptides ◽  
Molecular Design ◽  
Design And Synthesis

A Solid-Phase Synthetic Route to Unnatural Amino Acids with Diverse Side-Chain Substitutions

2002 ◽  
Vol 67 (9) ◽  
pp. 2960-2969 ◽  
Author(s):  
William L. Scott ◽  
Martin J. O'Donnell ◽  
Francisca Delgado ◽  
Jordi Alsina
Keyword(s):  
Amino Acids ◽  
Unnatural Amino Acids ◽  
Solid Phase ◽  
Side Chain ◽  
Synthetic Route

A New and Efficient Synthesis of Unnatural Amino Acids and Peptides by Selective 3,3-Dimethyldioxirane Side-Chain Oxidation

1999 ◽  
Vol 64 (23) ◽  
pp. 8468-8474 ◽  
Author(s):  
Raffaele Saladino ◽  
Maurizio Mezzetti ◽  
Enrico Mincione ◽  
Ines Torrini ◽  
Mario Paglialunga Paradisi ◽  
...  
Keyword(s):  
Amino Acids ◽  
Unnatural Amino Acids ◽  
Side Chain ◽  
Efficient Synthesis ◽  
Chain Oxidation

Synthesis of Azido Acids and Their Application in the Preparation of Complex Peptides

Synthesis ◽  
2020 ◽  
Author(s):  
Ryan Moreira ◽  
Michael Noden ◽  
Scott D. Taylor
Keyword(s):  
Amino Acids ◽  
Natural Products ◽  
Total Synthesis ◽  
Cyclic Peptides ◽  
Protecting Groups ◽  
Side Chain ◽  
Coupling Reactions ◽  
Protecting Group

AbstractAzido acids are important synthons for the synthesis of complex peptides. As a protecting group, the azide moiety is atom-efficient, easy to install and can be reduced in the presence of many other protecting groups, making it ideal for the synthesis of branched and/or cyclic peptides. α-Azido acids are less bulky than urethane-protected counterparts and react more effectively in coupling reactions of difficult-to-form peptide and ester bonds. Azido acids can also be used to form azoles on complex intermediates. This review covers the synthesis of azido acids and their application to the total synthesis of complex peptide natural products.1 Introduction2 Synthesis of α-Azido Acids2.1 From α-Amino Acids or Esters2.2 Via α-Substitution2.3 Via Electrophilic Azidation2.4 Via Condensation of N-2-Azidoacetyl-4-Phenylthiazolidin- 2-Thi one Enolates with Aldehydes and Acetals2.5 Synthesis of α,β-Unsaturated α-Azido Acids and Esters3 Synthesis of β-Azido Acids3.1 Preparation of Azidoalanine and 3-Azido-2-aminobutanoic Acids3.2 General Approaches to Preparing β-Azido Acids Other Than Azi doalanine­ and AABA4 Azido Acids in Total Synthesis4.1 α-Azido Acids4.2 β-Azido Acids and Azido Acids Containing an Azide on the Side Chain5 Conclusions

Solid-phase synthesis and utilization of side-chain reactive unnatural amino acids

2003 ◽  
Vol 44 (46) ◽  
pp. 8403-8406 ◽  
Author(s):  
Martin J. O'Donnell ◽  
Jordi Alsina ◽  
William L. Scott
Keyword(s):  
Amino Acids ◽  
Unnatural Amino Acids ◽  
Solid Phase Synthesis ◽  
Solid Phase ◽  
Side Chain ◽  
Phase Synthesis

ChemInform Abstract: Molecular Design and Synthesis of Artificial Ion Channels Based on Cyclic Peptides Containing Unnatural Amino Acids.

ChemInform ◽  
2010 ◽  
Vol 32 (34) ◽  
pp. no-no
Author(s):  
Hitoshi Ishida ◽  
Zhi Qi ◽  
Masahiro Sokabe ◽  
Kiyoshi Donowaki ◽  
Yoshihisa Inoue
Keyword(s):  
Amino Acids ◽  
Ion Channels ◽  
Unnatural Amino Acids ◽  
Cyclic Peptides ◽  
Molecular Design ◽  
Design And Synthesis

scholarly journals The Effect of a Peptide Substrate Containing an Unnatural Branched Amino Acid on Chymotrypsin Activity

Processes ◽  
2021 ◽  
Vol 9 (2) ◽  
pp. 242
Author(s):  
Yuuki Yamawaki ◽  
Tomoki Yufu ◽  
Tamaki Kato
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Substrate Specificity ◽  
Unnatural Amino Acids ◽  
Side Chain ◽  
Low Molecular Weight ◽  
Amino Acid Residues ◽  
Phase Synthesis ◽  
Reaction Velocity ◽  
Natural Amino Acids

7-Amino-4-methylcoumarin (AMC) is a low molecular weight fluorescent probe that can be attached to a peptide to enable the detection of specific proteases, such as chymotrypsin, expressed in certain diseases. Because this detection depends on the specificity of the protease toward the peptidyl AMC, the development of specific substrates is required. To investigate the specificity of chymotrypsin, peptidyl AMC compounds incorporating four different amino acid residues were prepared by liquid-phase synthesis. Two unnatural amino acids, 2-amino-4-ethylhexanoic acid (AEH) and cyclohexylalanine (Cha), were used to investigate the substrate specificity as these amino acids have structures different from natural amino acids. AEH was synthesized using diethyl acetamidemalonate as a starting material. The substrate containing Cha had high hydrophobicity and showed a high reaction velocity with chymotrypsin. Although the AEH substrate with a branched side chain had high hydrophobicity, it showed a low reaction velocity. The substrate containing the aromatic amino acid phenylalanine was less hydrophobic than the Cha and AEH substrates, but chymotrypsin showed the highest specificity for this compound. These results demonstrated that the substrate specificity of chymotrypsin is not only affected by the hydrophobicity and aromaticity, but also by the structural expanse of amino acid residues in the substrate.

scholarly journals Synthetic, structural and biological studies of the ubiquitin system: synthesis and crystal structure of an analogue containing unnatural amino acids

1997 ◽  
Vol 323 (3) ◽  
pp. 727-734 ◽  
Author(s):  
Steven G. LOVE ◽  
Tom W. MUIR ◽  
Robert RAMAGE ◽  
Kevin T. SHAW ◽  
Dmitriy ALEXEEV ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Amino Acids ◽  
Unnatural Amino Acids ◽  
Side Chain ◽  
Hydrophobic Core ◽  
Biological Behaviour ◽  
Methyl Group ◽  
Ubiquitin System ◽  
Biological Studies ◽  
The Stability

Ubiquitin is a 76-amino acid protein involved in the targeting for destruction of proteins in the cell. The protein can readily be synthesized chemically affording an extra dimension to studies of protein stability. Ubiquitin with various modifications to the hydrophobic core has been synthesized. In particular, two core amino acids have been replaced by aminobutyric acid (Val-26) and norvaline (for Ile-30) and the product crystallized. The refined crystal structure shows an overall contraction of the molecule and the side chain of Nva-30 rotates relative to Ile-30. However, the side chain rotation is not sufficient to compensate for the effect of the loss of the methyl group and hence a small cavity is introduced into the structure, which decreases the stability of the protein. The biological behaviour of the modified protein is unaltered. The observed changes in stability are of the magnitude expected for the removal of methyl groups from the hydrophobic core of a protein. Interestingly, the effect appears to be independent of the position of the removed methyl group. The intact structure, but not its stability, is important for recognition by the biological conjugating system.

scholarly journals In vivo modulation of ubiquitin chains by N-methylated non-proteinogenic cyclic peptides

2021 ◽  
Author(s):  
Joseph M. Rogers ◽  
Mickal Nawatha ◽  
Betsegaw Lemma ◽  
Ganga B. Vamisetti ◽  
Ido Livneh ◽  
...  
Keyword(s):  
Amino Acids ◽  
Unnatural Amino Acids ◽  
Cyclic Peptides ◽  
In Cells

Cyclic peptides containing unnatural amino acids can modulate Lys-48 ubiquitin chains in cells and animals.

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