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PP3 f(119-135) [id=LAP0003]

Producer Organism : Native Protein : Production Method :
Cow PP3 Synthetic
Activity : Not determined
Target Organisms :

Unavailable data

Description :
Production method: Synthetic.

LAP0001 and LAP0003 peptides both interact with phospholipids, but only LAP0001 can incorporate into planar lipidic bilayers by forming voltage-dependent channels. The conductance levels indicate that channel formation may be achieved by association of 4 to 6 bundles of peptides according to the barrelstave model (Citation 1).
Citation: 1

Antibacterial activity of lactophoricin, a synthetic 23-residues peptide derived from the sequence of bovine milk component-3 of proteose peptone

Cited Entries: LAP0001, LAP0003

Authors:Campagna, S., Mathot, A.G., Fleury, Y., Girardet, J.M., Gaillard, J.L.
Journal: Journal of Dairy Science 2004, 87(6).
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Abstract: A synthetic peptide of 23 residues corresponding to the carboxyterminal 113 to 135 region of component-3 of proteose peptone (PP3) has been investigated with regard to its antibacterial properties. This cationic amphipathic peptide that we refer to as lactophoricin, displayed a growth-inhibitory activity against both gram-positive and gram-negative bacteria. For most of the strains tested, bacterial growth was observed in the presence of lactophoricin except for Streptococcus thermophilus. In that case, lactophoricin exhibited a minimum inhibitory concentration of 10 μM and a minimum lethal concentration of 20 μM. No hemolysis of human red blood cells was detected for peptide concentrations between 2 to 200 μM, indicating that lactophoricin would be noncytotoxic when used in this concentration range.
Keywords: bovine milk; component-3 of proteose peptone; antimicrobial activity; amphipathic peptide
Citation: 2

Solution and solid-state NMR structural studies of antimicrobial peptides LPcin-I and LPcin-II

Cited Entries: LAP0001, LAP0003

Authors:Park, T.-J., Kim, J.-S., Ahn, H.-C., Kim, Y.
Journal: Biophysical Journal 2011, 101(5): 9.
Abstract: Lactophoricin (LPcin-I) is an antimicrobial, amphiphatic, cationic peptide with 23-amino acid residues isolated from bovine milk. Its analogous peptide, LPcin-II, lacks six N-terminal amino acids compared to LPcin-I. Interestingly, LPcin-II does not display any antimicrobial activity, whereas LPcin-I inhibits the growth of both Gram-negative and Gram-positive bacteria without exhibiting any hemolytic activity. Uniformly 15N-labeled LPcin peptides were prepared by the recombinant expression of fusion proteins in Escherichia coli, and their properties were characterized by electrospray ionization mass spectrometry, circular dichroism spectroscopy, and antimicrobial activity tests. To understand the structure-activity relationship of these two peptides, they were studied in model membrane environments by a combination of solution and solid-state NMR spectroscopy. We determined the tertiary structure of LPcin-I and LPcin-II in the presence of dodecylphosphorylcholine micelles by solution NMR spectroscopy. Magnetically aligned unflipped bicelle samples were used to investigate the structure and topology of LPcin-I and LPcin-II by solid-state NMR spectroscopy.

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