Search for the optimal mass profile of neuropeptides for the implementation of antihypoxic and activating actions

Abstract

In this study, the dependence of the pharmacological effects of neurotropic peptides of natural and synthetic origin on their structure was studied in laboratory rats. First, the study of the relative molecular profiles of peptide complexes was carried out using HPLC (gel-penetrating chromatography) with an internal standard. Then peptide complexes were administered to animals rectal and verified their biological activity on two independent models antihypoxic activity (method of altitude the lift timing of the animal's life at a critical height) and the model of assessment of physical performance (time of forced swim test of animals with a load of 10% of the body weight to failure). The obtained data on biological activity (increase) were compared with the features of the structure of peptides. To assess the effect of drug doses on their activity, a single-factor analysis of variance was performed.
 It has been shown that antihypoxic activity and performance stimulation are more or less inherent in all the studied peptide preparations, and are dose-dependent and related to the features of the molecular mass distribution of peptide components. It was also found that the specific antihypoxic activity of peptide preparations from brain tissues is associated with components having a mass range from 5 to 10 kDa. The optimal proportions of the peptide components for the implementation of biological activity by mass ranges were determined.
 In addition, the chromatographic characteristics (molecular weight distribution over mass ranges) of natural neuropeptide complexes can be used to predict the severity of their biological effects.

Related Papers

• → Determination of molecular mass of acidic polysaccharides by capillary electrophoresis(2002)12 cited
• → FMRFamide neuropeptides and neuropeptide-associated enzymes inDrosophila(1999)64 cited
• Neuropeptides : a methodology(1989)
• → Detection of Neuropeptides by lmmunocytochemistry(2003)10 cited
• Neuropeptides in the cat diencephalon: I. Thalamus(2001)