Exceptional adhesive and gelling properties of fibrous nanoscopic tapes of self-assembled bipolar urethane amides of L-phenylalanine

Seven L-phenylalanine based alkyl (monopolar) and alkanediyl (bipolar) derivatives are synthesized; while the bipolar urethane amides form gels and show strong adhesive properties, the monopolar analogues form fibrous nanoscopic cloth-like tapes.

Impressive Gelation in Organic Solvents by Synthetic, Low Molecular Mass, Self-Organizing Urethane Amides of L-Phenylalanine

Synthetic routes leading to 12 L-phenylalanine based mono- and bipolar derivatives (1-12) and an in-depth study of their structure-property relationship with respect to gelation have been presented. These include monopolar systems such as N-[(benzyloxy)carbonyl]-L-phenylalanine-N-alkylamides and the corresponding bipolar derivatives with flexible and rigid spacers such as with 1,12-diaminododecane and 4,4'-diaminodiphenylmethane, respectively. The two ends of the latter have been functionalized with N-[(benzyloxy)carbonyl]-L-phenylalanine units via amide connection. Another bipolar molecule was synthesized in which the middle portion of the hydrocarbon segment contained polymerizable diacetylene unit. To ascertain the role of the presence of urethane linkages in the gelator molecule protected L-phenylalanine derivatives were also synthesized in which the (benzyloxy)carbonyl group has been replaced with (tert-butyloxy)carbonyl, acetyl, and benzoyl groups, respectively. Upon completion of the synthesis and adequate characterization of the newly described molecules, we examined the aggregation and gelation properties of each of them in a number of solvents and their mixtures. Optical microscopy and electron microscopy further characterized the systems that formed gels. Few representative systems, which showed excellent gelation behavior was, further examined by FT-IR, calorimetric, and powder X-ray diffraction studies. To explain the possible reasons for gelation, the results of molecular modeling and energy-minimization studies were also included. Taken together these results demonstrate the importance of the presence of (benzyloxy)carbonyl unit, urethane and secondary amide linkages, chiral purities of the headgroup and the length of the alkyl chain of the hydrophobic segment as critical determinants toward effective gelation.

beta.-Turn conformation of N-acetyl-L-prolylglycyl-L-phenylalanine. Crystal structure and solution studies

Pro-Gly segments in peptides and proteins are prone to adopt the 0-turn conformation. This paper reports experimental data for the presence of this conformation in a linear tripeptide N-acetyl-L-prolylglycyl-L-phenylalanineb oth in the solid state and in solution. X-ray diffraction data on the tripeptide crystal show that it exists in the type I1 0-turn conformation. CD and proton NMR data show that this conformation persists in trifluoroethanol and methanol solutions in equilibrium with the nonhydrogen-bonded structures. Isomerization around the acetyl-prolyl bond is seen to take place in dimethyl sulfoxide solutions of the tripeptide.

Cinnamate toxicity expression on phenylalanine ammonia-lyase activity, germination and growth of cucumber (Cucumis sativis) seedlings

Cinnamate is the product of phenylalanine ammonialyase (PAL). This compound, a precursor of phenolics in plants, has been shown to be phytotoxic. Cinnamate inhibits PAL activity in cucumber seedlings. DL-phenylalanine has the same effect on the enzyme but does not affect growth. Actinomycin D and cycloheximide are phytotoxic and inhibit PAL. Production of a double-peg has been noticed in the seedlings, grown in the presence of actinomycin D. Light stimulates PAL activity in the seedling.

Decrease of phenylalanine hydroxylase during hepatocyte proliferation

In partially hepatectomized rats, the activity of phenylalanine hydroxylase decreased in the regenerating liver but not in the kidney. The concentration of corticosterone in the plasma of hepatectomized rats increased, and phenylalanine hydroxylase, despite being cortisol inducible, decreased in these as well as simultaneously adrenalectomized rats, showing lack of correlation between the changes of the steroid and the enzyme during the regeneration process. The decrease in the enzyme activity could be prevented by administering, during hepatic regeneration, only noradrenaline and adrenergic blocking agents, among the many hormones and phenyl compounds tested. A decrease in hepatic phenylalanine hydroxylase was also observed during two other conditions of hepatocyte cell proliferation obtained after giving chlorophenoxyisobutyrate and α-hexachlorocyclohexane.

Effect of environmental stress of low pressure on tyrosine aminotransferase and phenylalanine 4-hydroxylase activities in the rat.

Tyrosine aminotransferase activity in the liver increased about fourfold after 9h, on exposure of rats to stress of low pressure. 2. The phenylalanine hydroxylase activity increased about 60% on exposure for 24h or more. 3. An environmental pressure decrease of about 0.033 MN/m2 is needed to increase the activity of tyrosine aminotransferase. 4. Adrenalectomy completely abolished the increase in activity of tyrosine aminotransferase obtained on exposure to low pressure. 5. Treatment with cycloheximide or actinomycin D prevented the increase in activity of tyrosine aminotransferase. 6. Treatment with cycloheximide at the early part of exposure to stress prevented the increase in activity of phenylalanine hydroxylase obtained after 24h.

Metabolism of DL-(+/-)-phenylalanine by Aspergillus niger.

A fungus capable of degrading DL-phenylalanine was isolated from the soil and identified as Aspergillus niger. It was found to metabolize DL-phenylalanine by a new pathway involving 4-hydroxymandelic acid. D-Amino acid oxidase and L-phenylalanine: 2-oxoglutaric acid aminotransferase initiated the degradation of D- and L-phenylalanine, respectively. Both phenylpyruvate oxidase and phenylpyruvate decarboxylase activities could be demonstrated in the cell-free system. Phenylacetate hydroxylase, which required reduced nicotinamide adenine dinucleotide phosphate, converted phenylacetic acid to 2- and 4-hydroxyphenylacetic acid. Although 4-hydroxyphenylacetate was converted to 4-hydroxymandelate, 2-hydroxyphenylacetate was not utilized until the onset of sporulation. During sporulation, it was converted rapidly into homogentisate and oxidized to ring-cleaved products. 4-Hydroxymandelate was degraded to protocatechuate via

Microbial L-phenylalanine ammonia-lyase. Purification, subunit structure and kinetic properties of the enzyme from Rhizoctonia solani

Phenylalanine ammonia-lyase (EC 4.3.1.5) was purified to homogeneity from the acetone-dried powders of the mycelial felts of the plant pathogenic fungus Rhizoctonia solani. 2. A useful modification in protamine sulphate treatment to get substantial purification of the enzyme in a single-step is described. 3. The purified enzyme shows bisubstrate activity towards L-phenylalanine and L-tyrosine. 4. It is sensitive to carbonyl reagents and the inhibition is not reversed by gel filtration. 5. The molecular weight of the enzyme as determined by Sephadex G-200 chromatography and sucrose-density-gradient centrifugation is around 330000. 6. The enzyme is made up of two pairs of unidentical subunits, with a molecular weight of 70000 (alpha) and 90000 (beta) respectively. 7. Studies on initial velocity versus substrate concentration have shown significant deviations from Michaelis-Menten kinetics. 8. The double-reciprocal plots are biphasic (concave downwards) and Hofstee plots show a curvilinear pattern. 9. The apparent Km value increases from 0.18 mM to as high as 5.0 mM with the increase in the concentration of the substrate and during this process the Vmax, increases by 2-2.5-fold. 10. The value of Hill coefficient is 0.5. 11. Steady-state rates of phenylalanine ammonia-lyase reaction in the presence of inhibitors like D-phenylalanine, cinnamic, p-coumaric, caffeic, dihydrocaffeic and phenylpyruvic acid have shown that only one molecule of each type of inhibitor binds to a molecule of the enzyme. These observations suggest the involvement of negative homotropic interactions in phenylalanine ammonia-lyase. 12. The enzyme could not be desensitized by treatment with HgCl2, p-chloromercuribenzoic acid or by repeated freezing and thawing.

p-hydroxymandelic acid - a key intermediate in the metabolism of DL(+)-phenylalanine by aspergillus niger

The metabolism of phenylalanine by a strain of Aspergillus niger, isolated from the soil by enrichment culture has been studied. Analyses of the culture filtrates and replacement studies with various metabolites have revealed the operation of a degradative pathway involving p-hydroxymandelate as a key intermediate in this organism, p-Hydroxymandelate has been isolated from the cultural filtrates and its identity established by UV, IR and chromatographic techniques. A scheme for the degradation of phenylalanine in this organism has been proposed.