Synthesis of aspartic acid derivatives useful for the preparation of misacylated transfer RNAs

2000 ◽  
Vol 78 (6) ◽  
pp. 884-891 ◽  
Author(s):  
Michiel Lodder ◽  
Curtis F Crasto ◽  
Andrei L Laikhter ◽  
Haoyun An ◽  
Tuncer Arslan ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Aspartic Acid ◽  
Side Chain ◽  
Transfer Rnas ◽  
Rna Ligase ◽  
T4 Rna Ligase ◽  
In Vitro Transcripts ◽  
Derivatives Of

Several derivatives of aspartic acid were protected on Nα as their NVOC derivatives, and on the side chain carboxylates as nitroveratryl esters. Following activation as the cyanomethyl esters, these fully protected aspartate derivatives were converted to the respective pdCpA esters. The protected aspartyl-pdCpA esters were then utilized as substrates for T4 RNA ligase in the presence of in vitro transcripts of tRNA lacking the pCpA dinucleotide normally found at the 3'-end. In this fashion, several misacylated tRNAs were prepared; following photolytic deprotection, these were employed successfully for incorporation into proteins at predetermined positions.Key words: aminoacylated nucleotides, amino acid protection, protein synthesis, tRNA activation.

Geometric changes around an N atom due to a urethane-type bis(tert-butoxycarbonyl) substituent

2012 ◽  
Vol 69 (1) ◽  
pp. 82-86
Author(s):  
Dominika Wojewska ◽  
Alicja Kluczyk ◽  
Katarzyna Ślepokura
Keyword(s):  
Amino Acid ◽  
Crystal Structures ◽  
Aspartic Acid ◽  
Conformational Changes ◽  
Dimethyl Ester ◽  
Side Chain ◽  
Amino Acid Side Chain ◽  
Amino Group ◽  
Geometric Changes ◽  
Derivatives Of

Two crystal structures of urethane-protected derivatives of aspartic acid dimethyl ester are presented, namely dimethyl (2S)-2-[(tert-butoxycarbonyl)amino]butanedioate, C11H19NO6, and dimethyl (2S)-2-{bis[(tert-butoxycarbonyl]amino}butanedioate, C16H27NO8. The geometry at the N atom is discussed and compared with similar structures. The analysis of singly and doubly N-substituted derivatives reveals an elongation of all bonds involving the N atom and conformational changes of the amino acid side chain due to steric interactions with two bulky substituents on the amino group.

scholarly journals Novel Amino Acid Derivatives of Quinolines as Potential Antibacterial and Fluorophore Agents

2020 ◽  
Vol 88 (4) ◽  
pp. 57
Author(s):  
Oussama Moussaoui ◽  
Rajendra Bhadane ◽  
Riham Sghyar ◽  
El Mestafa El Hadrami ◽  
Soukaina El Amrani ◽  
...  
Keyword(s):  
Amino Acid ◽  
Methyl Esters ◽  
Amino Acid Derivatives ◽  
Bacterial Strains ◽  
Fluorescent Properties ◽  
Topoisomerase Iv ◽  
Microdilution Method ◽  
Hydrolysis Of ◽  
Derivatives Of

A new series of amino acid derivatives of quinolines was synthesized through the hydrolysis of amino acid methyl esters of quinoline carboxamides with alkali hydroxide. The compounds were purified on silica gel by column chromatography and further characterized by TLC, NMR and ESI-TOF mass spectrometry. All compounds were screened for in vitro antimicrobial activity against different bacterial strains using the microdilution method. Most of the synthesized amino acid-quinolines show more potent or equipotent inhibitory action against the tested bacteria than their correspond esters. In addition, many of them exhibit fluorescent properties and could possibly be utilized as fluorophores. Molecular docking and simulation studies of the compounds at putative bacterial target enzymes suggest that the antimicrobial potency of these synthesized analogues could be due to enzyme inhibition via their favorable binding at the fluoroquinolone binding site at the GyrA subunit of DNA gyrase and/or the ParC subunit of topoisomerase-IV.

scholarly journals Identification in skeletal muscle of a distinct extracellular pool of amino acids, and its role in protein synthesis

1971 ◽  
Vol 121 (5) ◽  
pp. 817-827 ◽  
Author(s):  
R. C. Hider ◽  
E. B. Fern ◽  
D. R. London
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Incubation Medium ◽  
Extensor Digitorum Longus ◽  
Extensor Digitorum ◽  
Longus Muscle ◽  
Kinetics Of

1. The kinetics of radioactive labelling of extra- and intra-cellular amino acid pools and protein of the extensor digitorum longus muscle were studied after incubations with radioactive amino acids in vitro. 2. The results indicated that an extracellular pool could be defined, the contents of which were different from those of the incubation medium. 3. It was concluded that amino acids from the extracellular pool, as defined in this study, were incorporated directly into protein.

Effect of Cycloheximide on In Vitro and In Vivo Protein Synthesis by Certain Tissues of Rats and Pigeons with Special Reference to Muscle

1973 ◽  
Vol 51 (12) ◽  
pp. 933-941 ◽  
Author(s):  
Njanoor Narayanan ◽  
Jacob Eapen
Keyword(s):  
Amino Acids ◽  
Body Weight ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Amino Acid Incorporation ◽  
Contrast Administration ◽  
Acid Incorporation ◽  
Tissue Homogenates

The effect of cycloheximide in vitro and in vivo on the incorporation of labelled amino acids into protein by muscles, liver, kidneys, and brain of rats and pigeons was studied. In vitro incorporation of amino acids into protein by muscle microsomes, myofibrils, and myofibrillar ribosomes was not affected by cycloheximide. In contrast, administration of the antibiotic into intact animals at a concentration of 1 mg/kg body weight resulted in considerable inhibition of amino acid incorporation into protein by muscles, liver, kidneys, and brain. This inhibition was observed in all the subcellular fractions of these tissues during a period of 10–40 min after the administration of the precursor. Tissue homogenates derived from in vivo cycloheximide-treated animals did not show significant alteration in in vitro amino acid incorporation with the exception of brain, which showed a small but significant enhancement.

scholarly journals Action of growth hormone in vitro on the net uptake and incorporation into protein of amino acids in muscle from intact rabbits given protein-deficient diets

1976 ◽  
Vol 35 (1) ◽  
pp. 1-10 ◽  
Author(s):  
M. R. Turner ◽  
P. J. Reeds ◽  
K. A. Munday
Keyword(s):  
Amino Acids ◽  
Growth Hormone ◽  
Protein Synthesis ◽  
Amino Acid ◽  
De Novo ◽  
Amino Acid Uptake ◽  
Acid Uptake ◽  
Amino Acid Incorporation ◽  
Acid Incorporation

1. Net amino acid uptake, and incorporation into protein have been measured in vitro in the presence and absence of porcine growth hormone (GH) in muscle from intact rabbits fed for 5 d on low-protein (LP), protein-free (PF) or control diets.2. In muscle from control and LP animals GH had no effect on the net amino acid uptake but stimulated amino acid incorporation into protein, although this response was less in LP animals than in control animals.3. In muscle from PF animals, GH stimulated both amino acid incorporation into protein and the net amino acid uptake, a type of response which also occurs in hypophysectomized animals. The magnitude of the effect of GH on the incorporation of amino acids into protein was reduced in muscle from PF animals.4. The effect of GH on the net amino acid uptake in PF animals was completely blocked by cycloheximide; the uptake effect of GH in these animals was dependent therefore on de novo protein synthesis.5. It is proposed that in the adult the role of growth hormone in protein metabolism is to sustain cellular protein synthesis when there is a decrease in the level of substrate amino acids, similar to that which occurs during a short-term fast or when the dietary protein intake is inadequate.

Effect of Dietary Protein and Amino Acid Mixture on Protein Synthesis in vitro in Rat Liver

1974 ◽  
Vol 16 (6) ◽  
pp. 325-336 ◽  
Author(s):  
Alexandra von der Decken ◽  
Per T. Omstedt
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Rat Liver ◽  
Dietary Protein ◽  
Amino Acid Mixture ◽  
Acid Mixture

In vitro studies on the inhibition of colon cancer by amino acid derivatives of bromothiazole

2017 ◽  
Vol 27 (15) ◽  
pp. 3507-3510 ◽  
Author(s):  
Nuno Vale ◽  
Ana Correia-Branco ◽  
Bárbara Patrício ◽  
Diana Duarte ◽  
Fátima Martel
Keyword(s):  
Colon Cancer ◽  
Amino Acid ◽  
In Vitro Studies ◽  
Amino Acid Derivatives ◽  
Derivatives Of

scholarly journals Biotin-mediated protein biosynthesis

1974 ◽  
Vol 140 (3) ◽  
pp. 549-556 ◽  
Author(s):  
R. L. Boeckx ◽  
K. Dakshinamurti
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Rat Liver ◽  
Intestinal Mucosa ◽  
Protein Biosynthesis ◽  
Amino Acid Incorporation ◽  
Acid Incorporation ◽  
Stimulation Of

The effect of administration of biotin to biotin-deficient rats on protein biosynthesis was studied. Biotin treatment resulted in stimulation by more than twofold of amino acid incorporation into protein, both in vivo and in vitro in rat liver, pancreas, intestinal mucosa and skin. Analysis of the products of amino acid incorporation into liver proteins in vivo and in vitro indicated that the synthesis of some proteins was stimulated more than twofold, but others were not stimulated at all. This indicates a specificity in the stimulation of protein synthesis mediated by biotin.

scholarly journals Pyridyl-Ala Modified Cyclic Hexapeptides: In-Vitro and In-Vivo Profiling for Oral Bioavailability

2019 ◽  
Vol 26 (3) ◽  
pp. 1383-1397 ◽  
Author(s):  
Thomas Vorherr ◽  
Ian Lewis ◽  
Joerg Berghausen ◽  
Felix Huth ◽  
Michael Schaefer ◽  
...  
Keyword(s):  
Amino Acid ◽  
Oral Bioavailability ◽  
Side Chain ◽  
Pyridyl Nitrogen ◽  
Oral Uptake ◽  
Cyclic Hexapeptides ◽  
Chain Interaction

Abstract We and others have been aiming at modifications to maintain or to enhance solubility while enabling permeability for cyclic hexapeptides. Especially, the 2-pyridyl-Ala modification was investigated, since in this case, the pyridyl-nitrogen is able to form an H-bond to the NH of the same residue. The hypothesis of a backbone side-chain interaction was demonstrated by NMR experiments, and further results obtained on a variety of pyridyl-Ala derivatives, studied systematically in the context of permeability, are presented in this contribution. Thus, this study sheds some more light on the pyridyl-Ala modification, which had been reported earlier. In addition to the in vitro profiling, the extent of oral bioavailability was assessed in rats. In principle, the pyridyl-Ala residue can be considered as an amino acid supporting oral uptake. Graphic Abstract

scholarly journals Identification of Mimotope Peptides Which Bind to the Mycotoxin Deoxynivalenol-Specific Monoclonal Antibody

1999 ◽  
Vol 65 (8) ◽  
pp. 3279-3286 ◽  
Author(s):  
Qiaoping Yuan ◽  
James J. Pestka ◽  
Brandon M. Hespenheide ◽  
Leslie A. Kuhn ◽  
John E. Linz ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Alkaline Phosphatase ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Synthetic Peptide ◽  
Amino Acid Sequences ◽  
In Vitro Translation ◽  
Enzyme Linked Immunosorbent Assay ◽  
Translation System

ABSTRACT Monoclonal antibody 6F5 (mAb 6F5), which recognizes the mycotoxin deoxynivalenol (DON) (vomitoxin), was used to select for peptides that mimic the mycotoxin by employing a library of filamentous phages that have random 7-mer peptides on their surfaces. Two phage clones selected from the random peptide phage-displayed library coded for the amino acid sequences SWGPFPF and SWGPLPF. These clones were designated DONPEP.2 and DONPEP.12, respectively. The results of a competitive enzyme-linked immunosorbent assay (ELISA) suggested that the two phage displayed peptides bound to mAb 6F5 specifically at the DON binding site. The amino acid sequence of DONPEP.2 plus a structurally flexible linker at the C terminus (SWGPFPFGGGSC) was synthesized and tested to determine its ability to bind to mAb 6F5. This synthetic peptide (designated peptide C430) and DON competed with each other for mAb 6F5 binding. When translationally fused with bacterial alkaline phosphatase, DONPEP.2 bound specifically to mAb 6F5, while the fusion protein retained alkaline phosphatase activity. The potential of using DONPEP.2 as an immunochemical reagent in a DON immunoassay was evaluated with a DON-spiked wheat extract. When peptide C430 was conjugated to bovine serum albumin, it elicited antibody specific to peptide C430 but not to DON in both mice and rabbits. In an in vitro translation system containing rabbit reticulocyte lysate, synthetic peptide C430 did not inhibit protein synthesis but did show antagonism toward DON-induced protein synthesis inhibition. These data suggest that the peptides selected in this study bind to mAb 6F5 and that peptide C430 binds to ribosomes at the same sites as DON.

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