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Antimicrobial peptides isolated from the venom of hymenopterous insect
Monincová, Lenka ; Čeřovský, Václav (advisor) ; Macek, Tomáš (referee) ; Fusek, Martin (referee)
Rapid development of bacterial resistance and multiresitance to conventional antibiotics has resulted in an intensive search for alternative antimicrobial agents. Antimicrobial peptides (AMPs) belong to promising anti-infective candidates since they do not development bacterial resistance. They kill microbes by disturbing or permeabilizing the cytoplasmic membrane, or may target putative key intracellular compartments. Their advantages include fast action and selectivity between prokaryotic and eukaryotic cells. We have isolated several novel AMPs from the venom of wild bees: halictines (HAL-1 and HAL-2) from Halictus sexcinctus, lasiocepsin (Las) from Lasioglossum laticeps and macropin (MAC-1) from Macropis fulvipes. They are active against Gram-positive and Gram- negative bacteria and against yeast Candida albicans. While halictines and macropin have moderate hemolytic activity, Las shows no hemolytic activity. A novel AMP was isolated also from the mucus of Xiphydria camelus. This AMP belongs to the category of insect defensins. It contains 55 amino acid residues, three disulphide bridges and its C-terminus is amidated. CD and NMR studies of HAL-1, HAL-2 and MAC-1 revealed propensity to form amphipathic α-helical structure in the presence of sodium dodecyl sulfate or trifluoroethanol. For the...
Novel biologically active peptides from the venom of the solitary bee Macropis fulvipes (HYMENOPTERA: MELITTIDAE)
Monincová, Lenka ; Slaninová, Jiřina ; Voburka, Zdeněk ; Hovorka, Oldřich ; Fučík, Vladimír ; Borovičková, Lenka ; Bednárová, Lucie ; Buděšínský, Miloš ; Straka, J. ; Čeřovský, Václav
Two peptides (macropine-1 and macropin-2) were isolated, their structure determined by Edman degradation and mass spectrometry, which exhibited potent antimicrobial activity against both Gram-positive and -negative bacteria and moderate hemolytic activity against rat erythrocytes. We prepared several MAC-1 analogs to study the effect of their structure on antimicrobial and hemolytic activities.

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