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1. Tsutsumi A, Javkhlantugs N, Kira A, Umeyama M, Kawamura I, Nishimura K, Ueda K, Naito A: Structure and orientation of bovine lactoferrampin in the mimetic bacterial membrane as revealed by solid-state NMR and molecular dynamics simulation. Biophys J; 2012 Oct 17;103(8):1735-43
NCI CPTC Antibody Characterization Program. NCI CPTC Antibody Characterization Program .

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Structure and orientation of bovine lactoferrampin in the mimetic bacterial membrane as revealed by solid-state NMR and molecular dynamics simulation.
  • Bovine lactoferrampin (LFampinB) is a newly discovered antimicrobial peptide found in the N1-domain of bovine lactoferrin (268-284), and consists of 17 amino-acid residues.
  • It is important to determine the orientation and structure of LFampinB in bacterial membranes to reveal the antimicrobial mechanism.
  • We therefore performed (13)C and (31)P NMR, (13)C-(31)P rotational echo double resonance (REDOR), potassium ion-selective electrode, and quartz-crystal microbalance measurements for LFampinB with mimetic bacterial membrane and molecular-dynamics simulation in acidic membrane. (31)P NMR results indicated that LFampinB caused a defect in mimetic bacterial membranes.
  • Ion-selective electrode measurements showed that ion leakage occurred for the mimetic bacterial membrane containing cardiolipin.
  • Quartz-crystal microbalance measurements revealed that LFampinB had greater affinity to acidic phospholipids than that to neutral phospholipids. (13)C DD-MAS and static NMR spectra showed that LFampinB formed an α-helix in the N-terminus region and tilted 45° to the bilayer normal.
  • REDOR dephasing patterns between carbonyl carbon nucleus in LFampinB and phosphorus nuclei in lipid phosphate groups were measured by (13)C-(31)P REDOR and the results revealed that LFampinB is located in the interfacial region of the membrane.
  • Molecular-dynamics simulation showed the tilt angle to be 42° and the rotation angle to be 92.5° for Leu(3), which are in excellent agreement with the experimental values.
  • [MeSH-major] Lactoferrin / chemistry. Molecular Dynamics Simulation. Nuclear Magnetic Resonance, Biomolecular. Peptide Fragments / chemistry. Unilamellar Liposomes / chemistry
  • [MeSH-minor] Amino Acid Motifs. Cardiolipins / chemistry. Ion-Selective Electrodes

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  • [Copyright] Copyright © 2012 Biophysical Society. Published by Elsevier Inc. All rights reserved.
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  • (PMID = 23083717.001).
  • [ISSN] 1542-0086
  • [Journal-full-title] Biophysical journal
  • [ISO-abbreviation] Biophys. J.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Cardiolipins; 0 / Peptide Fragments; 0 / Unilamellar Liposomes; 0 / lactoferrampin; EC 3.4.21.- / Lactoferrin
  • [Other-IDs] NLM/ PMC3475389
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