Conformational study of bovine lactoferricin in membrane-micking conditions by molecular dynamics simulation and circular dichroism.

Lactoferricins are potent antimicrobial peptides released by pepsin cleavage of Lactoferrins. Bovine Lactoferricin (LfcinB) has higher activity than the intact bovine Lactoferrin, and is the most active among the other Lactoferricins of human, murine and caprine origin. In the intact protein the fragment corresponding to LfcinB is in an helical conformation, while in water LfcinB adopts an amphipathic β-hairpin structure.

Lactoferrin derived peptides: mechanisms of action and their perspectives as antimicrobial and antitumoral agents.

Antimicrobial peptides, AMPs, exert their function acting mainly at the membrane level. In the wide AMPs panorama a particular position is occupied by lactoferrin derived peptides. They also possess antiviral, antifungal and antitumor activities and their parent molecules are available in several mammalian fluids and in dairy industries waste.

Pattern expression of glycan residues in AZT-treated K562 cells analyzed by lectin cytochemistry.

The present paper shows that human chronic myeloid (K562) cells exposed 3 h to 20 microM 3'-azido-3'-deoxythymidine (AZT) exhibit marked variations of the oligosaccharide moiety of glycoconjugates. These changes were analyzed by confocal fluorescence microscopy, upon incubation of control and AZT-treated cells with biotin-lectin conjugates to visualize cell surface glycans or total glycans after cells permeabilization. In addition, cell fluorescence distribution of the biotinylated lectins, localized with streptavidin conjugates labeled with Alexa Fluor 488, was analyzed by flow cytometry.

Zidovudine inhibits protein kinase C activity in human chronic myeloid (K562) cells.

In this paper we show that human erythroleukaemia (K562) cells exhibited a significant inhibition of protein kinase C activity when cells were exposed to 40 micro M zidovudine in a time interval of 5-180 min., whereas prolonged treatment (24 hr) was uneffective. The addition of an excess of thymidine (125:1, mol:mol), in the cell suspension with or without zidovudine fully restored the protein kinase C activity.

Proteins pattern alteration in AZT-treated K562 cells detected by two-dimensional gel electrophoresis and peptide mass fingerprinting.

In this study we report the effect of AZT on the whole protein expression profile both in the control and the AZT-treated K562 cells, evidenced by two-dimensional gel electrophoresis and peptide mass fingerprinting analysis. Two-dimensional gels computer digital image analysis showed two spots that appeared up-regulated in AZT-treated cells and one spot present only in the drug exposed samples. Upon extraction and analysis by peptide mass fingerprinting, the first two spots were identified as PDI-A3 and stathmin, while the third one was proved to be NDPK-A.