Citation (#346):

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

Authors: Park, T.-J., Kim, J.-S., Ahn, H.-C., Kim, Y.

Journal: Biophysical Journal 2011, 101(5): 9.


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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