The subject of these studies was synthesis and determination of biological properties of a series of insect peptides, such as alloferon, Any-GS and their analogues. The synthesis of 14 peptides was performed by the solid-phase method. Biological effect of these peptides was evaluated by the antiviral test against Human Herpes Virus type 1 (HHV-1) in vitro using a Vero cell line. It was found that the investigated peptides inhibit the replication of HHV-1 in Vero cells.
A comprehensive overview of the recent state of the art of insect peptide hormones with chemical structures is presented. An increased interest in insect neuropeptides and dynamic development of that research area has been influenced by a rapid improvement of instrumentation necessary for isolation and structural characterization. Several research teams have studied the relationships between biological properties of insect and vertebrate peptide hormones (96-98). Thus hormones from the AKH family can be considered glucagon counterparts, whereas the myotropic hormones such as proctolin and Lem-PK (LPK) are a substance P equivalent. Insect melanization hormones Bom-MRCH in their structural characteristics and properties resemble those of mammal MSH, and leucosulfakinins Lem-SK-I and -11 show some similarities with gastrin I1 and cholecystokinin. Bombyxin-I1 (Born-PTTH-11) reveals a structural homology with human insulin and similar biological properties to adenocorticotropic mammal hormone. Allatostatin (Dip-JHS-I) may be compared to somatostatin as it can be inferred from the observations (99) that this peptide modulates JH secretion in cockroach, Blattella germanica. Determination of the primary structure of eclosion hormones Mas-EH and Born-EH-I1 as well as the amino acid sequence of allatotropin and allatostatin is a significant contribution to the understanding of the molecular mechanisms of metamorphosis and insect development.
The subject of our studies was the synthesis, biological evaluation, and conformational studies of insect tridecapeptide alloferon (H-His-Gly-Val-Ser-Gly-His-Gly-Gln-His-Gly-Val-His-Gly-OH) and its analogues such as: [des-His(1) ]-, [Lys(1) ]-, [Arg(1) ]-, and [Ala(1) ]-alloferon. These peptides were synthesized to check the influence of the His residue at position 1 of the alloferon chain on its antiviral activity. Two aspects of the biological effects of these peptides were determined: (i) the cytotoxicity in vitro in the Vero, LLC-MK2, and HEp-2 cell lines, and (ii) the antiviral activity in vitro in respect to DNA and RNA viruses. We found that alloferon inhibited the herpes virus multiplication and failed to affect the coxsackie virus replication, whereas [Lys(1) ]-alloferon exhibited a high inhibitory action towards both viruses. Moreover, the peptides did not show any cytotoxic activity against the Vero, LLC-MK2, and HEp-2 cells. The preliminary circular dichroism conformational studies showed that the peptides investigated seem to prefer an unordered conformation.
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