PMID- 22108318
OWN - NLM
STAT- MEDLINE
DCOM- 20120427
LR  - 20201209
IS  - 1873-2941 (Electronic)
IS  - 0009-3084 (Linking)
VI  - 165
IP  - 1
DP  - 2012 Jan
TI  - Comparative study on the interaction of cell-penetrating polycationic polymers 
      with lipid membranes.
PG  - 51-8
LID - 10.1016/j.chemphyslip.2011.11.002 [doi]
AB  - Cell-penetrating peptides are arginine- and lysine-rich cationic peptides that 
      can readily enter cells not only by themselves but also carrying other 
      macromolecular cargos. In fact, we have reported that polycationic polymer such 
      as poly-l-lysine (PLL) and poly-l-arginine (PLA) translocate through negatively 
      charged phospholipid liposome membranes. In this work, we made a comparative 
      study of the interaction of PLL or PLA with lipid membranes consisting of 
      negatively charged phospholipids to understand the role of basic amino acid 
      residue (i.e. arginine and lysine) in the membrane-penetrating activity of 
      polypeptides. PLA and PLL translocated into giant unilamellar vesicle composed of 
      soybean phospholipids. zeta-potential and turbidity measurements demonstrated the 
      electrostatic binding of PLL and PLA to large unilamellar vesicle (LUV). 
      Fluorescence studies using membrane probes revealed that the binding of PLA and 
      PLL to LUV affects the hydration and packing of the membrane interface region, in 
      which the membrane insertion of PLA appeared to be greater than PLL. Differential 
      scanning calorimetry showed that the enthalpy of the gel to liquid-crystalline 
      phase transition for dipalmitoyl phosphatidylglycerol vesicle was greatly reduced 
      by binding of PLL and PLA, in which the reduction is much larger in PLA than in 
      PLL. Circular dichroism measurements in 2,2,2-trifluoroethanol/water mixture or 
      in the presence of LUV indicated that the propensity of PLA to form alpha-helical 
      structure is greater than PLL. Consistently, attenuated total reflection-Fourier 
      transform infrared spectroscopy revealed that there is greater alpha-helical 
      structure in PLA bound to LUV compared to PLL, which has much less ordered 
      structure. Furthermore, isothermal titration calorimetry measurements 
      demonstrated that the contribution of enthalpy to the energetics of binding to 
      LUV is two-fold larger in PLA than in PLL. These results suggest that the 
      stronger interaction of arginine residue with negatively charged phospholipid 
      membranes compared to lysine residue appears to facilitate the conformational 
      change in cationic polypeptide and its insertion into lipid membrane interior.
CI  - Copyright (c) 2011 Elsevier Ireland Ltd. All rights reserved.
FAU - Takechi, Yuki
AU  - Takechi Y
AD  - Institute of Health Biosciences, The University of Tokushima Graduate School of 
      Pharmaceutical Sciences, 1-78-1 Shomachi, Tokushima 770-8505, Japan.
FAU - Tanaka, Hirokazu
AU  - Tanaka H
FAU - Kitayama, Hiroki
AU  - Kitayama H
FAU - Yoshii, Haruka
AU  - Yoshii H
FAU - Tanaka, Masafumi
AU  - Tanaka M
FAU - Saito, Hiroyuki
AU  - Saito H
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20111112
PL  - Ireland
TA  - Chem Phys Lipids
JT  - Chemistry and physics of lipids
JID - 0067206
RN  - 0 (Lipid Bilayers)
RN  - 0 (Peptides)
RN  - 0 (Phosphatidylglycerols)
RN  - 0 (Phospholipids)
RN  - 0 (Polyamines)
RN  - 0 (Polyelectrolytes)
RN  - 0 (Unilamellar Liposomes)
RN  - 0 (polycations)
RN  - 25104-18-1 (Polylysine)
RN  - 25212-18-4 (polyarginine)
RN  - VA9U6BR3SB (1,2-dipalmitoylphosphatidylglycerol)
SB  - IM
MH  - Calorimetry, Differential Scanning
MH  - Circular Dichroism
MH  - Lipid Bilayers/*chemistry/metabolism
MH  - Peptides/*chemistry
MH  - Phase Transition
MH  - Phosphatidylglycerols/chemistry
MH  - Phospholipids/chemistry
MH  - Polyamines/*chemistry
MH  - Polyelectrolytes
MH  - Polylysine/*chemistry
MH  - Spectroscopy, Fourier Transform Infrared
MH  - Static Electricity
MH  - Unilamellar Liposomes/chemistry
EDAT- 2011/11/24 06:00
MHDA- 2012/04/28 06:00
CRDT- 2011/11/24 06:00
PHST- 2011/09/08 00:00 [received]
PHST- 2011/11/02 00:00 [revised]
PHST- 2011/11/04 00:00 [accepted]
PHST- 2011/11/24 06:00 [entrez]
PHST- 2011/11/24 06:00 [pubmed]
PHST- 2012/04/28 06:00 [medline]
AID - S0009-3084(11)00349-5 [pii]
AID - 10.1016/j.chemphyslip.2011.11.002 [doi]
PST - ppublish
SO  - Chem Phys Lipids. 2012 Jan;165(1):51-8. doi: 10.1016/j.chemphyslip.2011.11.002. 
      Epub 2011 Nov 12.