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- Holm, T, et al.
(författare)
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Comparison of CPP uptake methods
- 2011
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Ingår i: Methods in molecular biology (Clifton, N.J.). - Totowa, NJ : Humana Press. - 1940-6029. ; 683, s. 207-17
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Tidskriftsartikel (refereegranskat)
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- Nekhotiaeva, N., et al.
(författare)
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Cell entry and antimicrobial properties of eukaryotic cell-penetrating peptides
- 2003
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Ingår i: The FASEB Journal. - : Wiley. - 0892-6638 .- 1530-6860. ; 17:15, s. 394-
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Tidskriftsartikel (refereegranskat)abstract
- Antimicrobial drug action is limited by both microbial and host cell membranes. Microbes stringently exclude the entry of most drugs, and mammalian membranes limit drug distribution and access to intracellular pathogens. Recently, cell-penetrating peptides (CPPs) have been developed as carriers to improve mammalian cell uptake. Given that CPP's are cationic and often amphipathic, similar to membrane active antimicrobial peptides, it may be possible to use CPP activity to improve drug delivery to microbes. Here, two CPPs, TP10 and pVEC, were found to enter a range of bacteria and fungi. The uptake route involves rapid surface accumulation within minutes followed by cell entry. TP10 inhibited Candida albicans and Staphylococcus aureus growth, and pVEC inhibited Mycobacterium smegmatis growth at low micromolar doses, below the levels that harmed human HeLa cells. Therefore, although TP10 and pVEC entered all cell types tested, they preferentially damage microbes, and this effect was sufficient to clear HeLa cell cultures from noninvasive S. aureus infection. Also, conversion of the cytotoxicity indicator dye SYTOX Green showed that TP10 causes rapid and lethal permeabilization of S. aureus and pVEC permeabilizes M. smegmatis, but not HeLa cells. Therefore, TP10 and pVEC can enter both mammalian and microbial cells and preferentially permeabilize and kill microbes.
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- Ostenson, CG, et al.
(författare)
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Galparan: a powerful insulin-releasing chimeric peptide acting at a novel site
- 1997
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Ingår i: Endocrinology. - : The Endocrine Society. - 0013-7227 .- 1945-7170. ; 138:8, s. 3308-3313
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Tidskriftsartikel (refereegranskat)abstract
- Galparan is a 27-amino acid long chimeric peptide, GWTLNSAGYLLGP-INLKALAALAKKIL amide, consisting of galanin-(1–13) linked to mastoparan amide via a peptide bond to provide the mastoparan and galanin effector parts of the molecules. Galparan (10μ m) powerfully stimulates insulin secretion from isolated rat pancreatic islets in a reversible and dose-dependent manner; the stimulation is 26-fold at 3.3 mm glucose and 6-fold at 16.7 mm glucose. Galparan also enhances insulin secretion to a similar extent from islets of diabetic GK rats. The stimulatory effect of galparan on insulin release is not directly dependent on extracellular Ca2+, nor can it be explained only by changes in free cytosolic Ca2+ concentrations. Furthermore, galparan is effective in evoking insulin release in B cells depolarized by 25 mm KCl when ATP-sensitive K+ channels are kept open by diazoxide. Thus, galparan, like mastoparan, stimulates exocytosis of insulin at a distal site in the stimulus-secretion coupling of the B cell. This distal site is not identical to that used by mastoparan, as pertussis toxin pretreatment does not influence the insulinogenic effect of galparan. In conclusion, galparan evokes a large and reversible insulin secretion, acting at a yet unknown distal site and also promoting exocytosis in depolarized B cells from normal rats as well as diabetic GK rats.
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- Öhman, Anders, et al.
(författare)
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A study of melittin, motilin and galanin in reversed micellar environments, using circular dichroism spectroscopy.
- 1996
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Ingår i: Biophysical Chemistry. - 0301-4622 .- 1873-4200. ; 59:1-2
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Tidskriftsartikel (refereegranskat)abstract
- Circular dichroism spectroscopy has been used to study the behaviour of the cytolytic peptide melittin, the intestinal peptide hormone motilin (porcine) and the neuropeptide galanin (porcine) in various reversed micellar systems. The micellar systems used contained sodium dodecyl sulphate, bis(2-ethylhexyl) sulfosuccinate, n-dodecyltrimethylammonium chloride or polyoxyethylene(7) lauryl ether. Various structural changes of the peptides, induced either by varying the water content or the surface charge of the reversed micelles, could be monitored. Melittin has in all micellar systems a large amount of alpha-helix, and is almost unaffected by both water content and the surface charge of the reversed micelles. Motilin on the other hand attains an alpha-helical structure at low water content only. The surface charges seem to be of importance for the association between motilin and the hydrated reversed micellar surface. Galanin has the most complicated behaviour with a large dependence on surface charge and with a water content dependence which varies with the surfactant used. Stabilization of alpha-helical secondary structures was only seen in negatively charged reversed micelles. These observations indicate a specific interaction between galanin and surfactant, probably of electrostatic nature.
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| 50. |
- Öhman, Anders, et al.
(författare)
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NMR study of the conformation and localization of porcine galanin in SDS micelles. Comparison with an inactive analog and a galanin receptor antagonist.
- 1998
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Ingår i: Biochemistry. - : American Chemical Society (ACS). - 0006-2960 .- 1520-4995. ; 37:25
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Tidskriftsartikel (refereegranskat)abstract
- Galanin is a 29/30-residue neuro-endocrine peptide which performs its many important physiological functions via a membrane-bound receptor. By using two-dimensional proton NMR spectroscopy, complete relaxation matrix analysis, and simulated annealing, the conformation of porcine galanin was determined in a membrane-mimicking solvent containing sodium dodecyl sulfate (SDS) micelles. The final family of calculated structures displays three well-defined beta- or gamma-turn regions, comprising residues 1-5, 7-10, and 24-27, but has otherwise a random conformation. The receptor-interacting N-terminal part, residues 1-5, was found to be best defined with a backbone RMSD value of 0.12 A. The mode of association between galanin and the SDS micelle was determined by observing the broadening effect on proton resonances, when spin-labeled 5- and 12-doxyl stearate molecules were added. It was concluded that galanin is located close to the surface of the micelle with two regions, residues 6-9 and 24-29, as well as two single residues, 18 and 21, reaching out into the aqueous solvent. Additional NMR studies were carried out on an inactive analogue, Ala2-galanin, and an antagonist M40. The results show that the proton resonances of galanin and M40 have identical chemical shifts in the N-terminal receptor-interacting region, indicating similar solution structures in this region. For Ala2-galanin, the same region displays a spectral heterogeneity with chemical shifts clearly different from the other two peptides, indicative of different secondary structures. These results may provide a structural background for the antagonist activity of M40 and the hormonal inactivity of Ala2-galanin, as compared to galanin.
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