drosocin and Hemolysis

drosocin has been researched along with Hemolysis* in 4 studies

Other Studies

4 other study(ies) available for drosocin and Hemolysis

ArticleYear
Comparing naturally occurring glycosylated forms of proline rich antibacterial peptide, Drosocin.
    Glycoconjugate journal, 2017, Volume: 34, Issue:5

    Antimicrobial peptides (AMPs) are key players of innate immunity. Amongst various classes of AMPs, proline rich AMPs from insects enjoy special attention with few members of this class bearing O-glycosylation as post-translational modification. Drosocin, a 19 amino acid glycosylated AMP is a member of proline rich class, synthesized in the haemolymph of Drosophila melanogaster upon bacterial challenge. We report herein the chemical synthesis of drosocin carrying disaccharide (β-Gal(1 → 3)α-GalNAc) and comparison of its structural and functional properties with another naturally occurring monoglycosylated form of drosocin i.e. α-GalNAc-drosocin as well as with non-glycosylated drosocin. The disaccharide containing drosocin exhibited lower potency compared to monoglycosylated drosocin against all the tested Gram negative bacteria, suggesting the role of the distal sugar or increase in the sugar chain length on the activity. Circular dichroism studies failed to demonstrate the differential effect of sugars on the overall peptide conformation. Haemolytic and cytotoxic properties of drosocin were not altered due to an increase in the sugar chain length. In addition, we have also evaluated the effect of differentially glycosylated drosocins on two pro-inflammatory cytokines secreted by murine macrophages or LPS stimulated macrophages. All the drosocin forms tested, neither could stimulate the secretion of TNF-α and IL-6 nor could modulate LPS-induced levels of TNF-α and IL-6 in murine macrophages. This study provides insights about naturally occurring two different glycosylated forms of drosocin.

    Topics: Amino Acid Sequence; Animals; Anti-Bacterial Agents; Antimicrobial Cationic Peptides; Disaccharides; Drosophila melanogaster; Erythrocytes; Escherichia coli; Glycopeptides; Glycosylation; Hemolysis; Interleukin-6; Klebsiella pneumoniae; Lipopolysaccharides; Mice; Microbial Sensitivity Tests; Protein Processing, Post-Translational; Rats; RAW 264.7 Cells; Salmonella typhi; Salmonella typhimurium; Structure-Activity Relationship; Tumor Necrosis Factor-alpha

2017
Glycosylated analogs of formaecin I and drosocin exhibit differential pattern of antibacterial activity.
    Glycoconjugate journal, 2011, Volume: 28, Issue:8-9

    The synthetic glycopeptides are interesting model systems to study the effect of O-glycosylation in modulating their function and structure. A series of glycosylated analogs of two antibacterial peptides, formaecin I and drosocin, were synthesized by varying the nature of sugar and its linkage with bioactive peptides to understand the influence of structure variation of glycosylation on their antibacterial activities. Higher antibacterial activities of all glycopeptides compared to their respective non-glycosylated counterparts emphasize in part the importance of sugar moieties in functional implications of these peptides. The consequences of the unique differences among the analogs were apparent on their antibacterial activities but not evident structurally by circular dichroism studies. We have shown that differently glycosylated peptides exhibit differential effect among each other when tested against several Gram-negative bacterial strains. The change of monosaccharide moiety and/or its anomeric configuration in formaecin I and drosocin resulted into decrease in the antibacterial activity in comparison to that of the native glycopeptide, but the extent of decrease in antibacterial activity of glycosylated drosocin analogs was less. Probably, the variation in peptide conformation arising due to topological dissimilarities among different sugars in the same peptide resulting in possible modulation in binding properties appears to be responsible for differences in their antibacterial activities. Indeed, these effects of glycosylation are found to be sequence-specific and depend in the milieu of amino acid residues. Interestingly, none of the carbohydrate variants affected the basic property of these peptides, which is non-hemolytic and non-toxicity to eukaryotic cells.

    Topics: Amino Acid Sequence; Animals; Anti-Bacterial Agents; Antimicrobial Cationic Peptides; Bacteria; Carbohydrate Conformation; Carbohydrate Sequence; Cell Death; Circular Dichroism; Erythrocytes; Glycopeptides; Glycoproteins; Glycosylation; Hemolysis; Insect Proteins; Mice; Microbial Sensitivity Tests; Molecular Sequence Data; Rats

2011
Oncocin (VDKPPYLPRPRPPRRIYNR-NH2): a novel antibacterial peptide optimized against gram-negative human pathogens.
    Journal of medicinal chemistry, 2010, Jul-22, Volume: 53, Issue:14

    Small proline-rich antimicrobial peptides (AMP) have attracted considerable interest, as they target specific intracellular bacterial components and do not act by lytic mechanisms. Here, a novel peptide, termed oncocin (VDKPPYLPRPRPPRRIYNR-NH(2)), is reported that was optimized for the treatment of Gram-negative pathogens. Its minimal inhibitory concentrations in tryptic soy broth medium ranged from 0.125 to 8 microg/mL for 34 different strains and clinical isolates of Enterobacteriaceae and nonfermenters, such as Escherichia coli , Pseudomonas aeruginosa , and Acinetobacter baumannii . Substitutions of two arginine residues by ornithine increased the half-lives in full mouse serum from about 20 min to greater than 180 min and the activity. Both optimized oncocin derivatives were neither toxic to human cell lines nor hemolytic to human erythrocytes. They could freely penetrate lipid membranes and were washed out completely without any sign of lytic activity, as assessed by quartz crystal microbalance. Fluorescence labeled peptides entered the periplasmic space within 20 min at room temperature and homogeneously stained E. coli within 50 min. In conclusion, the optimized oncocin represents a very promising candidate for future in vivo work and may serve as a novel lead compound for an antibacterial drug class.

    Topics: Amino Acid Sequence; Animals; Anti-Bacterial Agents; Antimicrobial Cationic Peptides; Cell Line, Tumor; Cell Survival; Gram-Negative Bacteria; Hemolysis; Humans; Membranes, Artificial; Mice; Microbial Sensitivity Tests; Molecular Sequence Data; Peptides; Permeability; Structure-Activity Relationship

2010
Enlarged scale chemical synthesis and range of activity of drosocin, an O-glycosylated antibacterial peptide of Drosophila.
    European journal of biochemistry, 1996, May-15, Volume: 238, Issue:1

    Insects respond to a bacterial challenge by rapidly synthesizing a diverse range of antibacterial and antifungal peptides. One of them, drosocin, a 19-residue proline-rich antibacterial peptide, was isolated from Drosophila. This peptide carries a disaccharide moiety attached to a threonine residue in mid-chain position. The present report describes the enlarged-scale chemical synthesis of drosocin, glycosylated with Gal (beta 1 --> 3)GalNAc(alpha 1 --> O). We have studied the range of activity of the synthetic glycopeptide, of two truncated glycosylated isoforms, and of the unglycosylated L and D enantiomers. Both isolated and chemically synthesized drosocins carrying the disaccharide display the same antibacterial activity. Using circular dichroic spectroscopy we demonstrated that the O-linked disaccharidic motif did not affect the backbone conformation of drosocin. The antibacterial activity of the synthetic glycopeptide was directed against gram-negative strains with the exception of the gram-positive bacteria Micrococcus luteus. Deletion of the first five N-terminal residues completely abolished the activity of drosocin. As a first approach to the study of the mode of action of drosocin, we have synthesized a non-glycosylated D enantiomer and, using this molecule, we have shown that drosocin may act on the gram-negative bacteria through a stereospecific target.

    Topics: Amino Acid Sequence; Animals; Circular Dichroism; Drosophila; Glycopeptides; Glycosylation; Hemolysis; Isoenzymes; Microbial Sensitivity Tests; Molecular Sequence Data

1996