PMID- 21447320
OWN - NLM
STAT- MEDLINE
DCOM- 20110701
LR  - 20220330
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1808
IP  - 7
DP  - 2011 Jul
TI  - Binding of cell-penetrating penetratin peptides to plasma membrane vesicles 
      correlates directly with cellular uptake.
PG  - 1860-7
LID - 10.1016/j.bbamem.2011.03.011 [doi]
AB  - Cell-penetrating peptides (CPPs) gain access to intracellular compartments mainly 
      via endocytosis and have capacity to deliver macromolecular cargo into cells. 
      Although the involvement of various endocytic routes has been described it is 
      still unclear which interactions are involved in eliciting an uptake response and 
      to what extent affinity for particular cell surface components may determine the 
      efficiency of a particular CPP. Previous biophysical studies of the interaction 
      between CPPs and either lipid vesicles or soluble sugar-mimics of cell surface 
      proteoglycans, the two most commonly suggested CPP binding targets, have not 
      allowed quantitative correlations to be established. We here explore the use of 
      plasma membrane vesicles (PMVs) derived from cultured mammalian cells as cell 
      surface models in biophysical experiments. Further, we examine the relationship 
      between affinity for PMVs and uptake into live cells using the CPP penetratin and 
      two analogs enriched in arginines and lysines respectively. We show, using 
      centrifugation to sediment PMVs, that the amount of peptide in the pellet 
      fraction correlates linearly with the degree of cell internalization and that the 
      relative efficiency of all-arginine and all-lysine variants of penetratin can be 
      ascribed to their respective cell surface affinities. Our data show differences 
      between arginine- and lysine-rich variants of penetratin that has not been 
      previously accounted for in studies using lipid vesicles. Our data also indicate 
      greater differences in binding affinity to PMVs than to heparin, a commonly used 
      cell surface proteoglycan mimic. Taken together, this suggests that the cell 
      surface interactions of CPPs are dependent on several cell surface moieties and 
      their molecular organization on the plasma membrane.
CI  - Copyright (c) 2011 Elsevier B.V. All rights reserved.
FAU - Amand, Helene L
AU  - Amand HL
AD  - Department of Chemical and Biological Engineering, Chalmers University of 
      Technology, Gothenburg, Sweden.
FAU - Bostrom, Carolina L
AU  - Bostrom CL
FAU - Lincoln, Per
AU  - Lincoln P
FAU - Norden, Bengt
AU  - Norden B
FAU - Esbjorner, Elin K
AU  - Esbjorner EK
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20110405
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (Carrier Proteins)
RN  - 0 (Cell-Penetrating Peptides)
RN  - A2AQZ20TEK (penetratin)
SB  - IM
MH  - Animals
MH  - CHO Cells
MH  - Carrier Proteins/*metabolism
MH  - Cell Membrane/metabolism
MH  - Cell Membrane Permeability
MH  - Cell-Penetrating Peptides
MH  - Cricetinae
MH  - Cricetulus
MH  - Microscopy, Confocal
MH  - Protein Binding
EDAT- 2011/03/31 06:00
MHDA- 2011/07/02 06:00
CRDT- 2011/03/31 06:00
PHST- 2011/01/11 00:00 [received]
PHST- 2011/03/09 00:00 [revised]
PHST- 2011/03/21 00:00 [accepted]
PHST- 2011/03/31 06:00 [entrez]
PHST- 2011/03/31 06:00 [pubmed]
PHST- 2011/07/02 06:00 [medline]
AID - S0005-2736(11)00088-5 [pii]
AID - 10.1016/j.bbamem.2011.03.011 [doi]
PST - ppublish
SO  - Biochim Biophys Acta. 2011 Jul;1808(7):1860-7. doi: 10.1016/j.bbamem.2011.03.011. 
      Epub 2011 Apr 5.