Cellular Translocation of a γ-AApeptide Mimetic of Tat Peptide

2012 ◽  
Vol 9 (5) ◽  
pp. 1529-1534 ◽  
Author(s):  
Youhong Niu ◽  
Ge Bai ◽  
Haifan Wu ◽  
Rongsheng E. Wang ◽  
Qiao Qiao ◽  
...  
Keyword(s):  
Tat Peptide ◽  
Cellular Translocation

scholarly journals Synthesis and properties of G-quartet oligonucleotide-HIV-1 tat peptide conjugate

2006 ◽  
Vol 50 (1) ◽  
pp. 177-178
Author(s):  
Tetsuya Kumashiro ◽  
Toru Otake ◽  
Takuya Kawahata ◽  
Masao Akagi ◽  
Hidehito Urata
Keyword(s):  
Tat Peptide ◽  
Hiv 1

High-Efficiency Intracellular Magnetic Labeling with Novel Superparamagnetic-Tat Peptide Conjugates

1999 ◽  
Vol 10 (2) ◽  
pp. 186-191 ◽  
Author(s):  
Lee Josephson ◽  
Ching-Hsuan Tung ◽  
Anna Moore ◽  
Ralph Weissleder
Keyword(s):  
High Efficiency ◽  
Tat Peptide ◽  
Peptide Conjugates ◽  
Magnetic Labeling

scholarly journals A new method for direct detection of the sites of actin polymerization in intact cells and its application to differentiated vascular smooth muscle

2010 ◽  
Vol 299 (5) ◽  
pp. C988-C993 ◽  
Author(s):  
Hak Rim Kim ◽  
Paul C. Leavis ◽  
Philip Graceffa ◽  
Cynthia Gallant ◽  
Kathleen G. Morgan
Keyword(s):  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Actin Polymerization ◽  
Direct Detection ◽  
New Method ◽  
Actin Dynamics ◽  
Tat Peptide ◽  
Isolated Cells ◽  
Intact Cells ◽  
Permeabilized Cells

Here we report and validate a new method, suitable broadly, for use in differentiated cells and tissues, for the direct visualization of actin polymerization under physiological conditions. We have designed and tested different versions of fluorescently labeled actin, reversibly attached to the protein transduction tag TAT, and have introduced this novel reagent into intact differentiated vascular smooth muscle cells (dVSMCs). A thiol-reactive version of the TAT peptide was synthesized by adding the amino acids glycine and cysteine to its NH2-terminus and forming a thionitrobenzoate adduct: viz. TAT-Cys-S-STNB. This peptide reacts readily with G-actin, and the complex is rapidly taken up by freshly enzymatically isolated dVSMC, as indicated by the fluorescence of a FITC tag on the TAT peptide. By comparing different versions of the construct, we determined that the optimal construct for biological applications is a nonfluorescently labeled TAT peptide conjugated to rhodamine-labeled actin. When TAT-Cys-S-STNB-tagged rhodamine actin (TSSAR) was added to live, freshly enzymatically isolated cells, we observed punctae of incorporated actin at the cortex of the cell. The punctae are indistinguishable from those we have previously reported to occur in the same cell type when rhodamine G-actin is added to permeabilized cells. Thus this new method allows the delivery of labeled G-actin into intact cells without disrupting the native state and will allow its further use to study the effect of physiological intracellular Ca2+ concentration transients and signal transduction on actin dynamics in intact cells.

Closing the Loop: Constraining TAT Peptide by γPNA Hairpin for Enhanced Cellular Delivery of Biomolecules

2018 ◽  
Vol 29 (9) ◽  
pp. 2892-2898 ◽  
Author(s):  
Xiaohong Tan ◽  
Marcel P. Bruchez ◽  
Bruce A. Armitage
Keyword(s):  
Cellular Delivery ◽  
Tat Peptide ◽  
Closing The Loop
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