The architecture of Mourera fluviatilis (Podostemaceae): developmental morphology of inflorescences,flowers, and seedlings

Mourera fluviatilis from northern South America is a spectacular member of the Podostemaceae (river-weeds). Its raceme-like inflorescences are up to 64 cm long and have 40–90 flowers arranged in two opposite rows. Inflorescence development starts with the initiation of a double-sheathed (dithecous) bract in a terminal position. All lateral bracts (again dithecous) are initiated in basipetal order along the two flanks of the inflorescence. Each gap between two neighboring bracts contains a single flower. The flowers are bisexual, each with a whorl of 16–20 ligulate tepals and 14–40 stamens, which are arranged in one or two whorls. Floral development starts with the formation of a girdling primordium rim around a two-lobed primordial gynoecium. Stamen and tepal initiation is centrifugal on the girdling primordium. The anthers are introrse or extrorse, depending on stamen position. Seedlings develop two entire, threadlike cotyledons, followed by forked filamentous leaves, which arise from the plumular pole. The radicular pole of the hypocotyl develops into a claw-shaped holdfast that fixes the young plant to the rock. The developmental morphologies of Mourera fluviatilis and other members of the Mourera group (including Lonchostephus and Tulasneantha) fit well with the Podostemoideae bauplan known from other New World genera, such as Apinagia and Marathrum.     

14-membered cyclic opioids related to dermorphin and their partially retro-inverso modified analogues. I. Synthesis and biological activity.

As a continuation of our program to study structure-activity relationships of opiate peptides, we report the syntheses and biological activities of a series of 14-membered cyclic dermorphin analogues closely related to enkephalin analogue Tyr-c[D-A2bu-Gly-Phe-Leu] incorporating a phenylalanine at the third position in place of glycine. In addition to two parent dermorphin analogues Tyr-c[D-A2bu-Phe-Phe-(L and D)-Leu], four stereoisomeric retro-inverso modified analogues Tyr-c[D-A2bu-Phe-gPhe-(S and R)-mLeu] with a reversed amide bond between residues four and five, and Tyr-c[D-Glu-Phe-gPhe-(L and D)-rLeu] with two reversed amide bonds between residues four and five, and between residue five and the side chain of residue two have been synthesized. The results from the guinea pig ileum (GPI) and mouse vas deferens (MVD) assays show that all analogues are superactive at either one or both opiate receptors and in general display higher activities as compared to the corresponding enkephalin analogues with a glycine at the third position. Results from the in vitro biological assays and conformational analysis using 1H-NMR spectroscopy (adjoining paper) will provide useful information to understand the role of the Phe3 aromatic side chain in dermorphin, and that of the Phe4 aromatic side chain in enkephalin, on opiate activity since these cyclic dermorphin analogues contain two Phe residues at both the third and fourth positions.     

Aerobic and anaerobic carbohydrate metabolism and egg production of Schistosoma mansoni in vitro.

When S. mansoni adults were cultured in vitro for 12 days in a diphasic medium, their gross morphology, motor activity, frequency of sexual pairings, rates of glucose utilization and of lactic acid production were the same in the presence (90% N2/5% O2/5% CO2) or absence (95% N2/5% CO2) of oxygen. Therefore, no Pasteur effect, nor any reduction in lactic acid formation, was demonstrable under aerobic conditions. While aerobic conditions did not affect the rate of glycolysis, they had a marked effect on egg production. In the presence of oxygen, the rate of egg-laying reached a maximum between days 4 and 6. The average number of viable eggs produced per worm pair during this period was 118 (Sx equals 2.2), which is within the overall range (68 to 248) recorded by others for this same strain in vivo. Conversely, under anaerobic conditions in vitro, virtually no eggs were laid. It remains to be determined whether oxidative metabolism actually is required for energy to produce eggs, or whether some reaction yielding no ATP is essential for completion of their developmental process, such as tanning of the eggshall brought about by the oxidation of some phenolic compounds.     

Biological and conformational studies of [Val4]morphiceptin and [D-Val4]morphiceptin analogs incorporating cis-2-aminocyclopentane carboxylic acid as a peptidomimetic for proline

We report the synthesis, biological activity, and conformational analysis of tetrapeptide analogs related to [Val4]morphiceptin and [D-Val4]morphiceptin in which the proline at the second position has been replaced with cis-2-aminocyclopentane carboxylic acid (cis-2-Ac5c). Since the cis-2-Ac5c residue contains a normal amide, only the trans form has been observed about the amide bond between the first and second residues. The cis-2-Ac5c is a beta amino acid with two chiral centers resulting in two possible configurational isomers, namely (1S, 2R) and 1R, 2S) forms. The analogs containing the (1S, 2R)-Ac5c residue show activity at the mu-receptor but are inactive at the delta-receptor, resulting in a high selectivity for the mu-receptor. The (1R,2S)-Ac5c containing analogs are completely inactive at both the mu- and delta-receptors. The conformational analysis indicates that the separation of the aromatic rings of the tyrosine and phenylalanine residues, as expressed by the center-to-center distance, is 10.1-12.7 A for the preferred conformations of the bioactive analogs containing the (1S,2R)-Ac5c residue while a range of 4.8-7.0 A is observed for the preferred conformations of the inactive analogs with the (IR,2S)-Ac5c residue. A comparison of the findings from the conformational analysis and biological assays establishes the fact that a relatively large separation of the two aromatic side chains is required for the mu-opioid receptor activity of these molecules. Since the tetrapeptide amides studied in this investigation show similar biological profiles to those of the morphiceptin-related analogs, we have compared the preferred conformations estimated for the cis-2-Ac5c containing analogs with those of morphiceptin. One of the low energy conformations calculated for morphiceptin with the cis form about the tyrosine and proline residues has considerable topological similarity with the bioactive analogs containing the (1S,2R)-Ac5c residue, indicating that the cis from about these two residues is required for the biological activity of the morphiceptin-related analogs containing the proline at the second position.