Biologically active polypeptides of sea anemones: Structure, function, and prospects for application

2013 ◽  
Vol 39 (5) ◽  
pp. 311-320
Author(s):  
V. M. Tabakmakher ◽  
M. M. Monastyrnaya ◽  
E. V. Leichenko ◽  
I. N. Gladkikh ◽  
E. A. Zelepuga ◽  
...  
Author(s):  
Vladimir M. Mahnir ◽  
Uriy N. Shumilov ◽  
Alla M. Kovalevskaya ◽  
Liudmila A. Romanenko ◽  
Sergey D. Grebelny

2019 ◽  
Vol 3 (2) ◽  
pp. 117-136
Author(s):  
Kalina R.S. Monastyrnaya M.M.

Sea anemones are well-spread everywhere in the World Ocean and represent the most ancient active poisonous organisms. Their main instrument of attack on other animals are the nematocysts – stinging organelles with the curtailed hollow thread with poisonous edge on the end. In order to attract their potential victims, they use fluorescent proteins. These proteins became a separate object of research as genetically coded markers for the observation of activity of promotors of genes. The poisonous secret of sea anemones is characterized by the presence of maximum number of peptides of various structural classes and spatial structures among the studied land and marine organisms (bees, spiders, scorpions, snakes ect.). This fact complicates the identification of sea anemones' secret and its differentiation from poisons of animals of other taxons, if the concrete source of its origin is unknown. The toxicity of some biologically active sea anemone peptides (RpI, RpIII) at intravenous administration to experimental animals is comparable with that of the most well-known and dangerous representatives of natural toxins with the similar mechanism of action (an alpha-hemolysine and tetrodotoxin), or chemical warfare agents, such as sarin and hydrogen cyanide. Based on their toxic effect, the biologically active sea anemone peptides generally can be classified as neurotoxins due to their impact on the functioning of sodium channels in the cells of the nervous system of animals. cardiotoxic effect of sea anemone secret is caused by the specificity of interaction between its separate neurotoxins and one of the sub-types of sodium channels of muscle cells, characteristic for heart tissues. The main ways of identification of sea anemone neurotoxins in samples (for example, during the investigation of biological crimes) can be sequence by Edman`s method or tandem mass spectrometry (the analysis of fragments of toxin molecule for the establishment of its structure). Further study on the mechanisms of interaction between the sea anemone neurotoxins and the ion channels of the cells of nervous and muscular systems may result in the creation of medicines for treatment of channelopathy, as well as pluripotential antidotes, blocking the toxins, that influence on sodium channels


1999 ◽  
Vol 22 (3) ◽  
pp. 273-283 ◽  
Author(s):  
C Sen Gupta ◽  
RR Dighe

Human chorionic gonadotropin (hCG), a heterodimeric glycoprotein hormone, is composed of an alpha subunit noncovalently associated with the hormone-specific beta subunit. The objective of the present study was recombinant expression of properly folded, biologically active hCG and its subunits using an expression system that could be used for structure-function studies while providing adequate quantities of the hormone for immunocontraceptive studies. We report here expression of biologically active hCG and its subunits using a yeast expression system, Pichia pastoris. The recombinant hCGalpha and hCGbeta subunits were secreted into the medium and the levels of expression achieved at shake culture level were 24 and 2.7-3 mg/l secretory medium respectively. Co-expression of both subunits in the same cell resulted in secretion of heterodimeric hCG into the medium. The pichia-expressed hCG was immunologically similar to the native hormone, capable of binding to the LH receptors and stimulating a biological response in vitro. Surprisingly, the maximal response obtained was twice that obtained with the native hCG. The level of expression of hCG achieved was 12-16 mg/l secretory medium and is expected to increase several-fold in a fermentor. Thus the Pichia expression system is capable of hyperexpressing properly folded, biologically active hCG and is suitable for structure-function studies of the hormone.


Foods ◽  
2019 ◽  
Vol 8 (4) ◽  
pp. 131 ◽  
Author(s):  
Bolea ◽  
Grigore-Gurgu ◽  
Aprodu ◽  
Vizireanu ◽  
Stănciuc

The aim of this work was to advance knowledge on the potential use of black rice different sieving fractions for various functional applications, through proximate analysis, thermal degradation kinetics of phytochemical and characterization of the thermal behavior of the main proteins, from the perspectives of their use as a food ingredient. The results indicated that the thermal degradation of phytochemicals followed a first-order reaction kinetics for all the tested fractions. The temperature-dependent degradation was adequately modeled according to the Arrhenius equation. The calculated activation energies (Ea) and k values were different among the four studied parameters. The kinetic parameters depended on the grinding and sieving degree, the anthocyanins being the most thermolabile compounds, thus affecting the antioxidant activity. Three protein fractions were identified by electrophoresis with different molecular weight, such as albumin, globulin, and glutelin. The fluorescence spectroscopy experiments revealed the sequential character of the heat-induced conformational changes, different molecular events being suggested, such as folding in the lower temperature range and unfolding at higher temperature. The significance of the study is evidenced by the need to identify and advance the process-structure-function relationships for various biologically active compounds from the perspective of obtaining food or ingredients nutritionally optimized.


Peptides ◽  
1992 ◽  
Vol 13 (5) ◽  
pp. 851-857 ◽  
Author(s):  
Klaus Carstensen ◽  
Kenneth L. Rinehart ◽  
Ian D. McFarlane ◽  
Cornelis J.P. Grimmelikhuijzen

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