Faculty Opinions recommendation of Expanding the amino acid repertoire of ribosomal polypeptide synthesis via the artificial division of codon boxes.

2017 ◽  
Author(s):  
Gottfried Otting
Keyword(s):  
Amino Acid ◽  
Polypeptide Synthesis

scholarly journals Well-Defined Construction of Functional Macromolecular Architectures Based on Polymerization of Amino Acid Urethanes

Biomedicines ◽  
2020 ◽  
Vol 8 (9) ◽  
pp. 317
Author(s):  
Takeshi Endo ◽  
Atsushi Sudo
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Primary Amines ◽  
Amino Groups ◽  
Molecular Weights ◽  
Antifouling Coatings ◽  
Onium Salts ◽  
Polypeptide Synthesis ◽  
Produce Amino Acid ◽  
Derivatives Of

Polypeptide synthesis was accomplished using the urethane derivatives of amino acids as monomers, which can be easily prepared, purified, and stored at ambient temperature without the requirement for special precautions. The urethanes of amino acids are readily synthesized by the N-carbamoylation of onium salts of amino acids using diphenyl carbonate (DPC). The prepared urethanes are then efficiently cyclized to produce amino acid N-carboxyanhydrides (NCAs). Thereafter, in the presence of primary amines, the ring-opening polymerization (ROP) of NCAs is initiated using the amines, to yield polypeptides with controlled molecular weights. The polypeptides have propagating chains bearing reactive amino groups and initiating chain ends endowed with functional moieties that originate from the amines. Aiming to benefit from these interesting characteristics of the polypeptide synthesis using the urethanes of amino acids, various macromolecular architectures containing polypeptide components have been constructed and applied as biofunctional materials in highly efficient antifouling coatings against proteins and cells, as biosensors for specific molecules, and in targeted drug delivery.

scholarly journals The effect of hypermethylation on the functional properties of transfer ribonucleic acid. Ribosome-binding and polypeptide synthesis

1970 ◽  
Vol 119 (3) ◽  
pp. 587-593 ◽  
Author(s):  
J. Hay ◽  
D. J. Pillinger ◽  
E. Borek
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Binding Assay ◽  
Covalent Bond ◽  
Methyl Groups ◽  
Ribosome Binding ◽  
Phosphodiester Bonds ◽  
Polypeptide Synthesis ◽  
The Stability ◽  
Escherichia Coli B

1. Phenylalanyl-tRNA formed after chemical hypermethylation of Escherichia coli B tRNA was able to bind to ribosomes with the same efficiency as normal phenylalanyl-tRNA. 2. Under incubation conditions used in the ribosome-binding assay, hypermethylation of tRNA did not measurably decrease the stability of either inter-nucleotide phosphodiester bonds or the covalent bond between amino acid and tRNA in phenylalanyl-tRNA. 3. The ability of hypermethylated tRNA to take part in polyphenylalanine synthesis was inhibited progressively as the degree of hypermethylation increased. 4. Hypermethylation of tRNA affected polyphenylalanine synthesis at the stage of amino acid recognition and at a further point in the synthesis but not at the level of codon–anticodon recognition. 5. The formation of polylysine was more seriously affected by hypermethylation of tRNA than would be accounted for by inhibition of amino acid acceptance alone. 6. Polyproline formation was completely inhibited by the presence of 7mol% excess of methyl groups in tRNA. 7. The possibility of a link between amino acid acceptance and ribosome-binding was suggested for phenylalanyl-tRNA, but not for lysyl- or prolyl-tRNA.

Expanding the amino acid repertoire of ribosomal polypeptide synthesis via the artificial division of codon boxes

2016 ◽  
Vol 8 (4) ◽  
pp. 317-325 ◽  
Author(s):  
Yoshihiko Iwane ◽  
Azusa Hitomi ◽  
Hiroshi Murakami ◽  
Takayuki Katoh ◽  
Yuki Goto ◽  
...  
Keyword(s):  
Amino Acid ◽  
Polypeptide Synthesis

Alterations in the pattern of polypeptide synthesis resulting from amino acid limitation in Neurospora crassa

1988 ◽  
Vol 34 (10) ◽  
pp. 1166-1170 ◽  
Author(s):  
Harry J. Flint ◽  
Janis McKormick
Keyword(s):  
Amino Acid ◽  
Neurospora Crassa ◽  
Two Dimensional ◽  
Wild Type ◽  
Supply Rate ◽  
Limited Growth ◽  
Synthetic Enzymes ◽  
Two Dimensional Electrophoresis ◽  
Polypeptide Synthesis ◽  
Dimensional Electrophoresis

Two-dimensional electrophoresis was used to examine the pattern of polypeptide synthesis in Neurospora crassa mycelium of an arg-6 strain grown in the presence of [14C]arginine. Reduction in the arginine supply rate led to amino acid limited growth, and to major alterations in the pattern of polypeptide synthesis. Strains carrying wild-type (cpc-1+) or mutant (cpc-1) alleles at a locus governing cross-pathway control of amino acid synthetic enzymes differed markedly with respect to their pattern of polypeptide synthesis under limitation conditions, but differed little during arginine sufficient growth. Among 160 abundant polypeptide species classified for their response to limitation in two dimensional fluorographs, 31 were induced by limitation only in a cpc-1+ strain, 13 only in a cpc-1 strain, and 9 showed induction in both strains.

scholarly journals Synthesis of Polypeptides with High-Fidelity Terminal Functionalities under NCA Monomer-Starved Conditions

Research ◽  
2021 ◽  
Vol 2021 ◽  
pp. 1-16
Author(s):  
Lei Li ◽  
Jie Cen ◽  
Wenhao Pan ◽  
Yuben Zhang ◽  
Xuanxi Leng ◽  
...  
Keyword(s):  
Amino Acid ◽  
Primary Amine ◽  
Amine Hydrochloride ◽  
High Fidelity ◽  
Controlled Synthesis ◽  
General Strategy ◽  
Maldi Tof Ms ◽  
Block Copolypeptides ◽  
Polypeptide Synthesis ◽  
Tof Ms

Controlled polypeptide synthesis via α-amino acid N-carboxylic anhydride (NCA) polymerization using conventional primary amine initiators encounters two major obstacles: (i) normal amine mechanism (NAM) and activated monomer mechanism (AMM) coexist due to amine basicity and nucleophilicity and (ii) NCA is notoriously sensitive towards moisture and heat and unstable upon storage. We serendipitously discover that N-phenoxycarbonyl-functionalized α-amino acid (NPCA), a latent NCA precursor, could be polymerized solely based on NAM with high initiating efficiency by using primary amine hydrochloride as an initiator. The polymerization affords well-defined polypeptides with narrow polydispersity and high-fidelity terminal functionalities, as revealed by the clean set of MALDI-TOF MS patterns. We further demonstrate successful syntheses of random and block copolypeptides, even under open-vessel conditions. Overall, the integration of moisture-insensitive and air-tolerant NPCA precursors with stable primary amine hydrochloride initiators represents a general strategy for controlled synthesis of high-fidelity polypeptides with sophisticated functions.

NON-RIBOSOMAL POLYPEPTIDE SYNTHESIS

1973 ◽  
Vol 74 (Suppl) ◽  
pp. S294-S300 ◽  
Author(s):  
Fritz Lipmann
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Acid Activation ◽  
Bacillus Brevis ◽  
Amino Acid Activation ◽  
Molecular Weights ◽  
Polypeptide Synthesis ◽  
Secondary Transfer ◽  
Sequential Addition ◽  
Made In

ABSTRACT The biosynthesis of the cyclic decapeptide antibiotic, tyrocidine, was analyzed in particle-free supernatant fractions of RNase-treated homogenates of Bacillus brevis ATCC 8185. From the extracts, three complementary fractions with molecular weights of (1) 100 000, (2) 230 000, and (3) 440 000 were obtained. (1) activates and racemizes the initiating phenylalanine, (2) activates the three following amino acids, and (3) activates the last six amino acids by primary reaction with ATP to AMP-amino acid and secondary transfer to an enzyme-bound -SH. The enzymes alone fix amino acids but do not polymerize. The mixture, on sequential addition of amino acids + ATP, polymerizes first to enzyme-bound polypeptides, which after addition of all ten amino acids, cyclize. The enzymes (2) and (3) each contain one mole of 4'-phosphopantetheine which appears to act in transpeptidation. By mild autolysis and dodecyl sulphate gel electrophoresis, the polyenzymes may be split to subunits of 70 000 molecular weight, retaining only amino acid activation. In recent attempts to analyze the biosynthesis of the thyrotropic release hormone, a tripeptide made in the hypothalamus, we have met with great difficulties due to the presence of potent peptidases in brain preparations.

Sign in / Sign up

Export Citation Format

Share Document