Amino acid mediated mesopore formation in LTA zeolites

2016 ◽  
Vol 4 (6) ◽  
pp. 2305-2313 ◽  
Author(s):  
Zhuwen Chen ◽  
Jian Zhang ◽  
Bole Yu ◽  
Guangchao Zheng ◽  
Jing Zhao ◽  
...  
Keyword(s):  
Amino Acids ◽  
Hydrogen Bonding ◽  
Amino Acid ◽  
Mesoporous Zeolites ◽  
Calcination Step ◽  
Self Assembled

Amino acids, self-assembledin situ viahydrogen bonding, have been used to synthesize mesoporous zeolites without a calcination step.

A facile one pot route for the synthesis of imide tethered peptidomimetics

2016 ◽  
Vol 14 (2) ◽  
pp. 556-563 ◽  
Author(s):  
Veladi Panduranga ◽  
Girish Prabhu ◽  
Roopesh Kumar ◽  
Basavaprabhu Basavaprabhu ◽  
Vommina V. Sureshbabu
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Efficient Method ◽  
One Pot ◽  
Protected Amino Acid

A simple and efficient method for the synthesis of N,N’-orthogonally protected imide tethered peptidomimetics is presented. The imide peptidomimetics were synthesized by coupling the in situ generated selenocarboxylate of Nα-protected amino acids with Nα-protected amino acid azides in good yields.

Uptake and metabolism of amino acids by the dog liver perfused in situ

1962 ◽  
Vol 202 (3) ◽  
pp. 407-414 ◽  
Author(s):  
Rapier H. McMenamy ◽  
William C. Shoemaker ◽  
Jonas E. Richmond ◽  
David Elwyn
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Mixture ◽  
Acid Mixture ◽  
Sharp Rise ◽  
Dog Blood ◽  
Dog Liver ◽  
Amino Acid Concentrations ◽  
Uptake And Metabolism

Dog livers were perfused in situ for periods up to 6 hr with dog blood recycled through a pump-oxygenator. An amino acid mixture was administered for 90 min. Concentrations of amino acids were determined at intervals of 30 min or more. Rates of uptake and metabolism were calculated. After the start of perfusion, there is a fall in most plasma amino acid concentrations and a reciprocal rise in liver amino acids. Addition of amino acids causes a sharp rise in plasma amino acids. There is a rapid uptake of most of the amino acids by liver, although the concentrations of amino acids in liver fail to rise appreciably. Notable exceptions are valine, leucine, and isoleucine. Uptake of amino acids stimulates: a) an increase in the rate of synthesis of urea which ultimately accounts for 90% of the metabolized amino acids; b) a net synthesis of ornithine; and c) net noncatabolic metabolism of amino acids which may in part be protein synthesis. The results support the view that the liver temporarily stores a part of ingested amino acids as proteins, and subsequently makes them available to other organs.

Amino acid transport by juxtamedullary nephrons: distal reabsorption and recycling

1988 ◽  
Vol 255 (3) ◽  
pp. F397-F407 ◽  
Author(s):  
W. H. Dantzler ◽  
S. Silbernagl
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Transport ◽  
Acid Transport ◽  
Acidic Amino Acids ◽  
Vasa Recta ◽  
Collecting Ducts ◽  
Distal Site

Amino acid transport by juxtamedullary (JM) nephrons and its relationship to transport by superficial cortical (SC) nephrons and to function of vasa recta and collecting ducts were examined in vivo and in situ by free-flow micropuncture of Henle's loops, collecting ducts, and vasa recta and by continuous microinfusion of Henle's loops in exposed rat papillae. Fractional deliveries (FDs) of six neutral amino acids, two acidic amino acids, and taurine to tips of Henle's loops of JM nephrons could be substantially below those to early distal loops of SC nephrons, indicating that reabsorption before loop tips could be greater in JM than in SC nephrons. FDs to collecting ducts lower than to JM loop tips suggested reabsorption distal to loop tips. This was confirmed by continuous microinfusion of ascending limbs of Henle's loops. Distal site of reabsorption is unknown, but amino acids may move passively out of the thin ascending limb and be recycled into vasa recta and descending limb. Recycling of amino acids was supported by high FDs to tips of Henle's loops (sometimes greater than 1.0), higher concentrations in ascending than in descending vasa recta at same papilla level, and high mean concentrations in vasa recta.

X-ray studies on crystalline complexes involving amino acids and peptides. XL. Conformational variability, recurring and new features of aggregation, and effect of chirality in the malonic acid complexes of DL- and L-arginine

2002 ◽  
Vol 58 (6) ◽  
pp. 1051-1056 ◽  
Author(s):  
N. T. Saraswathi ◽  
M. Vijayan
Keyword(s):  
Amino Acids ◽  
Hydrogen Bonding ◽  
Amino Acid ◽  
Crystal Structures ◽  
Malonic Acid ◽  
Conformational Flexibility ◽  
X Ray ◽  
Conformational Variability ◽  
Aggregation Pattern ◽  
Positively Charged

The crystal structures of the complexes of malonic acid with DL- and L-arginine, which contain positively charged argininium ions and negatively charged semimalonate ions, further demonstrate the conformational flexibility of amino acids. A larger proportion of folded conformations than would be expected on the basis of steric consideration appears to occur in arginine, presumably because of the requirements of hydrogen bonding. The aggregation pattern in the DL-arginine complex bears varying degrees of resemblance to patterns observed in other similar structures. An antiparallel hydrogen-bonded dimeric arrangement of arginine, and to a lesser extent lysine, is a recurring motif. Similarities also exist among the structures in the interactions with this motif and its assembly into larger features of aggregation. However, the aggregation pattern observed in the L-arginine complex differs from any observed so far, which demonstrates that all the general patterns of amino-acid aggregation have not yet been elucidated. The two complexes represent cases where the reversal of the chirality of half the amino-acid molecules leads to a fundamentally different aggregation pattern.

Self-Assembled Copper–Amino Acid Nanoparticles for in Situ Glutathione “AND” H2O2 Sequentially Triggered Chemodynamic Therapy

2018 ◽  
Vol 141 (2) ◽  
pp. 849-857 ◽  
Author(s):  
Baojin Ma ◽  
Shu Wang ◽  
Feng Liu ◽  
Shan Zhang ◽  
Jiazhi Duan ◽  
...  
Keyword(s):  
Amino Acid ◽  
Self Assembled

scholarly journals Rumen degradability and ileal digestibility of proteins and amino acids of feedstuffs for cows

2014 ◽  
Vol 83 (3) ◽  
pp. 225-231
Author(s):  
Iveta Maskaľová ◽  
Vladimír Vajda ◽  
Marek Krempaský ◽  
Lukáš Bujňák
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Crude Protein ◽  
Amino Acid Profile ◽  
Ileal Digestibility ◽  
Corn Gluten ◽  
Corn Gluten Feed ◽  
Gluten Feed

Knowledge of the profile of amino acids of the rumen-undegradable protein can help in the formulation of diets to provide amino acids that complement microbial protein as well as supply amino acids, which are most limiting for milk production. Three non-lactating cows fitted with rumen cannulas were used to determine the effect ofin siturumen degradation on crude protein and amino acid profile of rumen-undegraded protein of feedstuffs. The obtained values of rumen degradability of crude protein with significant difference (P< 0.001) between feeds ranged from 20.3 to 76.3% (mean 62.0 ± 17.9%) and values of total amino acids ranged from 30.9% in corn gluten meal to 83.8% in corn gluten feed (mean 67.5 ± 16.4%). Anin vitromodified 3-step method was used to determine intestinal digestibility. Intestinal digestibility of undegraded protein varied from 54.5 ± 1.4% in raw soybean to 95.2 ± 1.0% in corn gluten feed. The absorbable amino acid profile of rumen-undegraded protein for each feedstuff was compared with profiles of the original feedstuff and the rumen-exposed undegraded protein. Absorbable lysine (9.3 ± 1.1 g/kg of crude protein) was higher in products of soybean and sunflower cake. Corn gluten feed and meal supplied more absorbable methionine (3.6 ± 0.6 g/kg of crude protein). This study showed that the digestibility factor of crude protein and amino acid based onin situandin vitromethods for thermal treatment of protein feeds can be used in models to optimize the amino acid nutrition of dairy cows and expand knowledge about rumen degradability and ileal digestibility of amino acids in feedstuffs.

Synthesis of functionalized pyrazole derivatives by regioselective [3+2] cycloadditions of N-Boc-α-amino acid-derived ynones

2018 ◽  
Vol 73 (7) ◽  
pp. 467-480 ◽  
Author(s):  
Eva Pušavec Kirar ◽  
Uroš Grošelj ◽  
Amalija Golobič ◽  
Franc Požgan ◽  
Sebastijan Ričko ◽  
...  
Keyword(s):  
Amino Acids ◽  
Nuclear Magnetic Resonance ◽  
Amino Acid ◽  
Ring Opening ◽  
Pyrazole Derivatives ◽  
X Ray Diffraction ◽  
X Ray ◽  
Acid Catalyzed ◽  
Azomethine Imines

Abstract [3+2] cycloadditions of ynones derived from glycine and (S)-alanine and some other dipolarophiles with azomethine imines, nitrile oxides, diazoacetate, and azidoacetate were studied. The dipolarophiles were obtained from α-amino acids, either by the reduction of the carboxy function with ethynylmagnesium bromide or by propiolation of the amino function. Cu-catalyzed cycloadditions of ynones to azomethine imines were regioselective and gave the expected cycloadducts as inseparable mixtures of diastereomers. In some instances, further oxidative hydrolytic ring-opening took place to afford 3,3-dimethyl-3-(1H-pyrazol-1-yl)propanoic acids. Acid-catalyzed cycloadditions of 3-butenone were also regioselective and provided mixtures of diastereomeric cycloadducts, which were separated by chromatography. In the reactions of title ynones with alkyl diazoacetates, in situ-formed benzonitrile oxides, and tert-butyl azidoacetate, all cycloadducts were obtained as single regioisomers. The structures of all novel compounds were established by nuclear magnetic resonance and X-ray diffraction.

Photochemistry of N-nitroso-N-alkyl amino acids: a facile oxidative decarboxylation

1980 ◽  
Vol 58 (23) ◽  
pp. 2477-2483 ◽  
Author(s):  
Yuan L. Chow ◽  
Douglas P. Horning ◽  
Joël Polo
Keyword(s):  
Amino Acids ◽  
Hydrogen Bonding ◽  
Acetic Acid ◽  
Amino Acid ◽  
Carboxyl Groups ◽  
Oxidative Decarboxylation ◽  
Solid States ◽  
Intramolecular Association

Several N-alkyl or N-phenyl-N-nitroso α-amino acids were synthesized and were shown to photolytically rearrange to amidoximes with concurrent decarboxylation in solution or solid states without the presence of externally added acids. In contrast, N-nitrosonipecotinic acid, a N-nitroso β-amino acid, as well as N-nitrosopiperidine in the presence of acetic acid were not photolabile. The photolability of N-nitroso α-amino acids was ascribed to the presence of an intramolecular association between the nitrosamino and carboxyl groups through hydrogen bonding. The species having the hydrogen bonding through the nitroso oxygen in the Z-configuration was believed to be photolabile and decomposed to alkylideneimines as the primary product. The mechanism of the oxidative photorearrangement was discussed.

Regulation of protein synthesis in lung by amino acids and insulin

1983 ◽  
Vol 245 (5) ◽  
pp. E508-E514
Author(s):  
J. M. Besterman ◽  
C. A. Watkins ◽  
D. E. Rannels
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Rat Plasma ◽  
Colloid Osmotic Pressure ◽  
Atp Depletion ◽  
Concentration Addition ◽  
Amino Acid Availability ◽  
Amino Acid Concentrations

Acute effects of amino acid availability and insulin on protein synthesis were investigated in rat lungs perfused in situ with buffer containing either 4.5% fraction V bovine serum albumin (FrV BSA), 4.5% essentially fatty acid-free (FAF) BSA, or 4.5% dextran to maintain colloid osmotic pressure. In the presence of FrV BSA, protein synthesis was unaffected by perfusion for 1 or 3 h with buffer containing no added amino acids (0X), as compared with amino acids at concentrations one (1X) or five (5X) times those in rat plasma. Regardless of the amino acid concentration, addition of insulin was without effect. Likewise, in lungs perfused for 1 h with either FAF BSA or dextran, protein synthesis was insensitive to amino acid availability or to insulin. After 3 h, however, protein synthesis decreased 34 and 37%, respectively, when these lungs were perfused in the absence of both amino acids and insulin. In both cases, the inhibition was prevented by addition of insulin to the perfusate; addition of the hormone to perfusate containing 1X amino acids or elevating perfusate amino acids to 5X did not affect protein synthesis. The deficit in protein synthesis observed in the absence of both amino acids and insulin was not accompanied by ATP depletion or by lower intracellular concentrations of amino acids. Similarly, the effect of insulin was not associated with a general elevation in intracellular amino acid concentrations.(ABSTRACT TRUNCATED AT 250 WORDS)

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