Cell-Penetrating, Dimeric α-Helical Peptides: Nanomolar Inhibitors of HIV-1 Transcription

2014 ◽  
Vol 126 (38) ◽  
pp. 10250-10253 ◽  
Author(s):  
Sangmok Jang ◽  
Soonsil Hyun ◽  
Seoyeon Kim ◽  
Seonju Lee ◽  
Im-Soon Lee ◽  
...  
2014 ◽  
Vol 53 (38) ◽  
pp. 10086-10089 ◽  
Author(s):  
Sangmok Jang ◽  
Soonsil Hyun ◽  
Seoyeon Kim ◽  
Seonju Lee ◽  
Im-Soon Lee ◽  
...  

2012 ◽  
Vol 9 (1) ◽  
pp. S94
Author(s):  
Shawn Keogan ◽  
Shendra Passic ◽  
Brian Wigdahl ◽  
Fred Krebs

2019 ◽  
Vol 41 (11) ◽  
pp. 1283-1298 ◽  
Author(s):  
Saba Davoodi ◽  
Azam Bolhassani ◽  
Seyed Mehdi Sadat ◽  
Shiva Irani

2020 ◽  
Vol 18 ◽  
pp. 145-158
Author(s):  
Pedro R.L. Perdigão ◽  
Catarina Cunha-Santos ◽  
Carlos F. Barbas ◽  
Mariana Santa-Marta ◽  
Joao Goncalves

2014 ◽  
Vol 25 (10) ◽  
pp. 1761-1768 ◽  
Author(s):  
Takuma Kato ◽  
Makoto Oba ◽  
Koyo Nishida ◽  
Masakazu Tanaka

2015 ◽  
Vol 112 (26) ◽  
pp. E3392-E3401 ◽  
Author(s):  
Sabina Sperandio ◽  
Corinne Barat ◽  
Miguel A. Cabrita ◽  
Ana Gargaun ◽  
Maxim V. Berezovski ◽  
...  

Target of Egr1 (TOE1) is a nuclear protein localized primarily in nucleoli and Cajal bodies that was identified as a downstream target of the immediate early gene Egr1. TOE1 displays a functional deadenylation domain and has been shown to participate in spliceosome assembly. We report here that TOE1 can function as an inhibitor of HIV-1 replication and show evidence that supports a direct interaction of TOE1 with the viral specific transactivator response element as part of the inhibitory mechanism. In addition, we show that TOE1 can be secreted by activated CD8+ T lymphocytes and can be cleaved by the serine protease granzyme B, one of the main components of cytotoxic granules. Both full-length and cleaved TOE1 can spontaneously cross the plasma membrane and penetrate cells in culture, retaining HIV-1 inhibitory activity. Antiviral potency of TOE1 and its cell-penetrating capability have been identified to lie within a 35-amino-acid region containing the nuclear localization sequence.


2007 ◽  
Vol 35 (4) ◽  
pp. 767-769 ◽  
Author(s):  
J. Howl ◽  
I.D. Nicholl ◽  
S. Jones

Studies of CPPs (cell-penetrating peptides), sequences that are also commonly designated as protein transduction domains, now extend to a second decade of exciting and far-reaching discoveries. CPPs are proven vehicles for the intracellular delivery of macromolecules that include oligonucleotides, peptides and proteins, low-molecular-mass drugs, nanoparticles and liposomes. The biochemical properties of different classes of CPP, including various sequences derived from the HIV-1 Tat (transactivator of transcription) [e.g. Tat-(48–60), GRKKRRQRRRPPQ], and the homeodomain of the Drosophila homeoprotein Antennapaedia (residues 43–58, commonly named penetratin, RQIKIWFQNRRMKWKK), also provide novel insights into the fundamental mechanisms of translocation across biological membranes. Thus the efficacy of CPP-mediated cargo delivery continues to provide valuable tools for biomedical research and, as witnessed in 2007, candidate and emerging therapeutics. Thus it is anticipated that the further refinement of CPP technologies will provide drug-delivery vectors, cellular imaging tools, nanoparticulate devices and molecular therapeutics that will have a positive impact on the healthcare arena. The intention of this article is to provide both a succinct overview of current developments and applications of CPP technologies, and to illustrate key developments that the concerted efforts of the many researchers contributing to the Biochemical Society's Focused Meeting in Telford predict for the future. The accompanying papers in this issue of Biochemical Society Transactions provide additional details and appropriate references. Hopefully, the important and eagerly anticipated biomedical and clinical developments within the CPP field will occur sooner rather than later.


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