Synthesis and structural investigation of 2-aminomethyl-3-(4-methoxy-phenyl)-propionic acid containing a peptide analogue of the amyloidogenic AS(6–7) sequence: inhibition of fibril formation

2017 ◽  
Vol 15 (19) ◽  
pp. 4218-4225 ◽  
Author(s):  
Arpita Paikar ◽  
Mintu Debnath ◽  
Debasish Podder ◽  
Supriya Sasmal ◽  
Debasish Haldar
Keyword(s):  
Amino Acid ◽  
Propionic Acid ◽  
Structural Investigation ◽  
Fibril Formation ◽  
Peptide Analogue ◽  
Phenyl Propionic Acid

The incorporation of a β-amino acid, namely 2-aminomethyl-3-(4-methoxy-phenyl)-propionic acid, inhibits amyloid-like fibril formation.

Identification of the gene encoding 3-(5-oxo-2-thioxoimidazolidin-4-yl) propionic acid desulfhydrase in Burkholderia sp. HME13

2020 ◽  
Vol 85 (3) ◽  
pp. 626-629
Author(s):  
Hisashi Muramatsu ◽  
Hiroki Maguchi ◽  
Taisuke Harada ◽  
Takehiro Kashiwagi ◽  
Chul-Sa Kim ◽  
...  
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Propionic Acid ◽  
Unknown Function ◽  
Protein Family ◽  
Amino Acid Sequence Analysis ◽  
Gene Encoding

ABSTRACT Here, we report the identification of the gene encoding a novel enzyme, 3-(5-oxo-2-thioxoimidazolidin-4-yl) propionic acid desulfhydrase, in Burkholderia sp. HME13. The enzyme converts 3-(5-oxo-2-thioxoimidazolidin-4-yl) propionic acid and H2O to 3-(2,5-dioxoimidazolidin-4-yl) propionic acid and H2S. Amino acid sequence analysis of the enzyme indicates that it belongs to the DUF917 protein family, which consists of proteins of unknown function.

scholarly journals Insights into the interactions and dynamics of a DES formed by phenyl propionic acid and choline chloride

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Parisa Jahanbakhsh Bonab ◽  
Alireza Rastkar Ebrahimzadeh ◽  
Jaber Jahanbin Sardroodi
Keyword(s):  
Diffusion Coefficient ◽  
Liquid Phase ◽  
Propionic Acid ◽  
Structural Parameters ◽  
Choline Chloride ◽  
Self Diffusion ◽  
Phenyl Propionic Acid ◽  
Donor And Acceptor ◽  
Experimental Values ◽  
Self Diffusion Coefficient

AbstractDeep eutectic solvents (DESs) have received much attention in modern green chemistry as inexpensive and easy to handle analogous ionic liquids. This work employed molecular dynamics techniques to investigate the structure and dynamics of a DES system composed of choline chloride and phenyl propionic acid as a hydrogen bond donor and acceptor, respectively. Dynamical parameters such as mean square displacement, liquid phase self-diffusion coefficient and viscosity are calculated at the pressure of 0.1 MPa and temperatures 293, 321 and 400 K. The system size effect on the self-diffusion coefficient of DES species was also examined. Structural parameters such as liquid phase densities, hydrogen bonds, molecular dipole moment of species, and radial and spatial distribution functions (RDF and SDF) were investigated. The viscosity of the studied system was compared with the experimental values recently reported in the literature. A good agreement was observed between simulated and experimental values. The electrostatic and van der Waals nonbonding interaction energies between species were also evaluated and interpreted in terms of temperature. These investigations could play a vital role in the future development of these designer solvents.

Fibril Formation of hsp10 Homologue Proteins and Determination of Fibril Core Regions: Differences in Fibril Core Regions Dependent on Subtle Differences in Amino Acid Sequence

2008 ◽  
Vol 377 (5) ◽  
pp. 1593-1606 ◽  
Author(s):  
Hisashi Yagi ◽  
Ai Sato ◽  
Akihiro Yoshida ◽  
Yoshiki Hattori ◽  
Masahiro Hara ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Fibril Formation

scholarly journals Preparation and Biological Activity of 2-(4-(Thiazol-2-yl)phenyl)propionic Acid Derivatives Inhibiting Cyclooxygenase.

1991 ◽  
Vol 39 (9) ◽  
pp. 2323-2332 ◽  
Author(s):  
Youichiro NAITO ◽  
Tomokazu GOTO ◽  
Fumihiko AKAHOSHI ◽  
Shiniciro ONO ◽  
Haruko YOSHITOMI ◽  
...  
Keyword(s):  
Biological Activity ◽  
Propionic Acid ◽  
Phenyl Propionic Acid

scholarly journals SPECIFICITY IN THE COMBINATION OF FD FRAGMENTS WITH L CHAINS TO FORM HAPTEN-BINDING SITES

1966 ◽  
Vol 123 (5) ◽  
pp. 921-934 ◽  
Author(s):  
O. A. Roholt ◽  
G. Radzimski ◽  
D. Pressman
Keyword(s):  
Amino Acid ◽  
Propionic Acid ◽  
Binding Sites ◽  
Amino Acid Analysis ◽  
Binding Activity ◽  
Light Chains ◽  
Antibody Activity ◽  
Fc Fragment ◽  
Fab Fragments ◽  
Correct Alignment

In the work reported here we have shown that light chains and Fd fragments can be separated completely in propionic acid and then recombined to form Fab fragments with antibody activity. This experiment indicates that in the recombination a correct alignment of the Fd fragments and the L chains occurs to give a competent antibody site, just as occurs with the recombination of separated heavy and light chains of the antibody; thus the Fc fragment is not required for correct alignment. Fd fragments of antibody alone show very low binding activity toward the specific hapten. As is the case for the combination of heavy and light chains, the combination of Fd fragments and light chains also requires that both components come from antibody from the same rabbit in order to give binding sites. When they are derived from different rabbits producing antibody against the same antigen, they still give Fab fragments as shown by immunoelectrophoresis but do not have competent binding sites. An important observation is that the subunits of the papain digest fractions, FabI and FabII, have the capacity to cross-combine to form active Fab fragments with competent binding sites. FdI from FabI combines with LII chains from FabII to give the composite (FdI-LII) with good binding activity. Likewise, the composite (FdII-LI) has good binding activity. The composites from the two types of antibody molecules yielding different Fab fragments have antibody activity although heretofore these molecules have appeared to be different on the bases of chromatography and amino acid analysis. There is also a preferential combination of the Fd fragments to combine with the correct L fragments to give binding sites since this combination takes preference over the combination of Fd fragments of antibody with light chains of normal globulin (or of light chains of antibody with Fd fragments of normal globulin).

Changes in amino acid compounds of wheat plants during ensiling and aerobic exposure: the influence of propionic acid and urea phosphate-calcium propionate

1984 ◽  
Vol 102 (3) ◽  
pp. 667-672 ◽  
Author(s):  
G. Ashbell ◽  
H. H. Theune ◽  
D. Sklan
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Glutamic Acid ◽  
Propionic Acid ◽  
Butyric Acid ◽  
Total Amino Acid ◽  
Amino Butyric Acid ◽  
Urea Phosphate ◽  
Fresh Material ◽  
Calcium Propionate

SummaryChanges in distribution of amino acid nitrogen of chopped wheat plants ensiled at shooting and flowering when wilted, and at the milk and dough stages as fresh material, were determined as affected by addition of 0·8% propionic acid (PrA) or 2·2% urea phosphate-calcium propionate (UP-CaPr). Analyses were carried out after an ensiling period of 90 days and after a further aerobic exposure period (AE) of 7 days.Total amino acid (TAA) contents in the dry matter (D.M.) during the fermentation period and in the AE were stable in untreated material (UM) and treated material. Concentration of essential amino acids decreased during fermentation, this decrease being higher in the UM. The free amino acids were low in the fresh material (18·6% of TAA) but increased in the ensiled material to ca. 71 % of the TAA in the silage. In the AE this level was 63% in UM and 69% in treated material. The ammonia-N contents increased during fermentation in UM and especially in the UP-CaPr treatments, while the opposite occurred in the PrA treatments.The concentrations of and changes in 21 amino acids (AAs) are given. The highest AA concentrations recorded in the fresh material were those of arginine, lysine, glutamic acid, alanine, leucine, proline and glycine. The most marked increments in AAs as a result of fermentation were those of ornithine, γ-amino butyric acid, threonine and methionine. Marked decreases were observed in glutamine, arginine and glutamic acid. PrA increased mainly arginine, asparagine and glutamine, whereas γ-amino butyric acid decreased; UP-CaPr increased arginine, asparagine, lysine and glutamic acid (in silage only) and reduced γ-amino butyric acid and glutamine (in AE only).

scholarly journals Impact of Fermentable Fibres on the Colonic Microbiota Metabolism of Dietary Polyphenols Rutin and Quercetin

2019 ◽  
Vol 16 (2) ◽  
pp. 292 ◽  
Author(s):  
Bahareh Mansoorian ◽  
Emilie Combet ◽  
Areej Alkhaldy ◽  
Ada L. Garcia ◽  
Christine Ann Edwards
Keyword(s):  
Gas Chromatography ◽  
Acetic Acid ◽  
Propionic Acid ◽  
Phenolic Acids ◽  
Gas Chromatography Mass Spectrometry ◽  
Phenyl Acetic Acid ◽  
Potential Health ◽  
Dietary Polyphenols ◽  
Colonic Microbiota ◽  
Phenyl Propionic Acid

Dietary fibre and polyphenols are both metabolised to short-chain fatty acids (SCFAs) and phenolic acids (PA) by the colonic microbiota. These may alter microbiota growth/diversity, but their interaction is not understood. Interactions between rutin and raftiline, ispaghula or pectin were investigated in human faecal batch cultures (healthy participants; 19–33 years, 4 males, 6 females, BMI 18.4–27.4) after a low (poly)phenol diet three days prior to study. Phenolic acids were measured by gas chromatography-mass spectrometry and SCFAs by gas chromatography-flame ionisation after 2, 4, 6, and 24 h. Rutin fermentation produced Phenyl acetic acid (PAA), 4-Hydroxy benzoic acid (4-OHBA), 3-Hydroxy phenyl acetic acid (3-OHPAA), 4-Hydroxy phenyl acetic acid (4-OHPAA), 3,4-Dihydroxy phenyl acetic acid (3,4-diOHPAA), 3-Hydroxy phenyl propionic acid (3-OHPPA), and 4-Hydroxy phenyl propionic acid (4-OHPPA). 3,4-DiOHPAA and 3-OHPAA were predominant at 6 h (1.9 ± 1.8 µg/mL, 2.9 ± 2.5 µg/mL, and 0.05 ± 0.0 µg/mL, respectively) and 24 h (5.5 ± 3.3 µg/mL, 3.1 ± 4.2 µg/mL, and 1.2 ± 1.6 µg/mL). Production of all PA except 3-OHPPA and 4-OHPPA was reduced by at least one fibre. Inhibition of PA was highest for rutin (8-fold, p < 0.01), then pectin (5-fold, p < 0.01), and ispaghula (2-fold, p = 0.03). Neither rutin nor quercetin had a detectable impact on SCFA production. These interactions should be considered when assessing dietary polyphenols and potential health benefits.

Sign in / Sign up

Export Citation Format

Share Document