Pharmacologically Active Peptides produced in the Tissues of the Host during Chronic Trypanosome Infections

Nature ◽  
1966 ◽  
Vol 212 (5058) ◽  
pp. 190-191 ◽  
Author(s):  
P. F. L. BOREHAM
Keyword(s):  
Active Peptides ◽  
Pharmacologically Active

scholarly journals Diversity of Conopeptides and Conoenzymes from the Venom Duct of the Marine Cone Snail Conus bayani as Determined from Transcriptomic and Proteomic Analyses

Marine Drugs ◽  
2021 ◽  
Vol 19 (4) ◽  
pp. 202
Author(s):  
Rajesh Rajaian Pushpabai ◽  
Carlton Ranjith Wilson Alphonse ◽  
Rajasekar Mani ◽  
Deepak Arun Apte ◽  
Jayaseelan Benjamin Franklin
Keyword(s):  
Gene Family ◽  
Transcriptome Sequencing ◽  
Cone Snail ◽  
Active Peptides ◽  
Transcriptomic Data ◽  
Sequencing Technologies ◽  
Hunting Strategies ◽  
Divergent Gene ◽  
Pharmacologically Active ◽  
Highly Evolved

Marine cone snails are predatory gastropods characterized by a well-developed venom apparatus and highly evolved hunting strategies that utilize toxins to paralyze prey and defend against predators. The venom of each species of cone snail has a large number of pharmacologically active peptides known as conopeptides or conotoxins that are usually unique in each species. Nevertheless, venoms of only very few species have been characterized so far by transcriptomic approaches. In this study, we used transcriptome sequencing technologies and mass spectrometric methods to describe the diversity of venom components expressed by a worm-hunting species, Conus bayani. A total of 82 conotoxin sequences were retrieved from transcriptomic data that contain 54 validated conotoxin sequences clustered into 21 gene superfamilies including divergent gene family, 17 sequences clustered to 6 different conotoxin classes, and 11 conotoxins classified as unassigned gene family. Seven new conotoxin sequences showed unusual cysteine patterns. We were also able to identify 19 peptide sequences using mass spectrometry that completely overlapped with the conotoxin sequences obtained from transcriptome analysis. Importantly, herein we document the presence of 16 proteins that include five post-translational modifying enzymes obtained from transcriptomic data. Our results revealed diverse and novel conopeptides of an unexplored species that could be used extensively in biomedical research due to their therapeutic potentials.

Pharmacologically Active Peptides and Proteins from Bee Venom

Animal Toxins ◽  
2000 ◽  
pp. 127-151
Author(s):  
Peter N. Strong ◽  
Jonathan D. F. Wadsworth
Keyword(s):  
Bee Venom ◽  
Active Peptides ◽  
Pharmacologically Active

scholarly journals Natural Bioactive Thiazole-Based Peptides from Marine Resources: Structural and Pharmacological Aspects

Marine Drugs ◽  
2020 ◽  
Vol 18 (6) ◽  
pp. 329
Author(s):  
Rajiv Dahiya ◽  
Sunita Dahiya ◽  
Neeraj Kumar Fuloria ◽  
Suresh Kumar ◽  
Rita Mourya ◽  
...  
Keyword(s):  
Binding Sites ◽  
Wide Spectrum ◽  
Structural Features ◽  
Complex Nature ◽  
Special Focus ◽  
Structural Components ◽  
Active Peptides ◽  
Peptide Interactions ◽  
Allosteric Binding Sites ◽  
Pharmacologically Active

Peptides are distinctive biomacromolecules that demonstrate potential cytotoxicity and diversified bioactivities against a variety of microorganisms including bacteria, mycobacteria, and fungi via their unique mechanisms of action. Among broad-ranging pharmacologically active peptides, natural marine-originated thiazole-based oligopeptides possess peculiar structural features along with a wide spectrum of exceptional and potent bioproperties. Because of their complex nature and size divergence, thiazole-based peptides (TBPs) bestow a pivotal chemical platform in drug discovery processes to generate competent scaffolds for regulating allosteric binding sites and peptide–peptide interactions. The present study dissertates on the natural reservoirs and exclusive structural components of marine-originated TBPs, with a special focus on their most pertinent pharmacological profiles, which may impart vital resources for the development of novel peptide-based therapeutic agents.

scholarly journals Comparative Analysis of Experimental Pharmacokinetics of New Neurotropic Peptides

2019 ◽  
Vol 2 (1) ◽  
Author(s):  
S.S. Boyko ◽  
V.P. Zherdev ◽  
R.V. Shevchenko ◽  
O.G. Gribakina
Keyword(s):  
Structural Features ◽  
New Drugs ◽  
Active Metabolites ◽  
Experimental Animals ◽  
Active Peptides ◽  
Nootropic Drug ◽  
Enzymatic Action ◽  
Enzymatic Systems ◽  
Glycine Ethyl Ester ◽  
Pharmacologically Active

Experimental pharmacokinetics of new pharmacologically active peptides, modified analogues of endogenous neuropeptides, has been investigated in rats and rabbits. The study icluded 3 new drugs: (i) the nootropic drug noopept (phenylacetyl-prolyl-glycine ethyl ester); (ii) dilept (N-caproyl-L-prolyl-L-tyrosine methyl ester) – the antipsychotic with positive mnemotropic action; (iii) compound GB-115 – selective anxiolytic (phenylhexanoyl-prolyl-tryptophan amide). Differences in pharmacokinetics and biotransformation of the studied drugs depended on their structural features. The ether derivatives noopept and dilept underwent intensive metabolism by rat gastrointestinal esterases and peptidases with the formation of active metabolites. Being an amide, the compound GB-115 was more resistant to the enzymatic effects of peptidases and was detected for a longer period in the blood of experimental animals. In rabbits the studied compounds were less exposed to the enzymatic action by gastrointestinal peptidases, and were detected plasma of rabbits for a longer period. The higher stability of the compounds studied in rabbits may be attributed not only to the structural features of the studied dipeptides, but also to differences in the activity of the enzymatic systems of the gastrointestinal tract participating in their metabolism, as well as differences in the rate of hepatic and renal blood flow in rats and rabbits.

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