Cell-penetrating peptides: mechanism and kinetics of cargo delivery

Zorko, Matjaž; Langel, Ülo

doi:10.1016/j.addr.2004.10.010

Cited by 745 publications

(610 citation statements)

References 87 publications

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“…Here, we have suggested a previously unknown function of amino acids derived from LPIN3 protein by identifying and characterizing a cell-penetrating peptide, which is located on its nuclear localization sequence. For over 20 years, various amino acids sequences of CPPs have been developed including penetratin (Antp), polylysine, polyarginine, TAT, VP22, and pep-1 (Deshayes et al, 2005;Heitz et al, 2009;Zorko and Langel, 2005). Many therapeutic cargo molecules have been successfully delivered into cells via CPPs including proteins, peptides, si-RNA, DNA, and others (van den Berg and Dowdy, 2011;Zorko and Langel, 2005).…”

Section: Discussionmentioning

confidence: 99%

“…For over 20 years, various amino acids sequences of CPPs have been developed including penetratin (Antp), polylysine, polyarginine, TAT, VP22, and pep-1 (Deshayes et al, 2005;Heitz et al, 2009;Zorko and Langel, 2005). Many therapeutic cargo molecules have been successfully delivered into cells via CPPs including proteins, peptides, si-RNA, DNA, and others (van den Berg and Dowdy, 2011;Zorko and Langel, 2005). TAT-BH4 and TAT-Bcl-XL inhibited sepsis-induced apoptosis of lymphocytes in vivo (Hotchkiss et al, 2006) and TAT-Cre was used to generate conditional knock-out mice (Wadia et al, 2004).…”

Section: Discussionmentioning

confidence: 99%

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Identification of a Novel Cell-Penetrating Peptide from Human Phosphatidate Phosphatase LpIN3

Lim

Kim

et al. 2012

Molecules and Cells

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Identification of a Novel Cell-Penetrating Peptide from Human Phosphatidate Phosphatase LpIN3

Lim

Kim

et al. 2012

Molecules and Cells

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“…TAT was used as a general targeting peptide because it binds rapidly and uniformly on the surface of cells (Fig. S1), and also enters many types through endocytosis (19). The second SBTuses the peptide Cys-RPARPAR, which specifically binds to a pocket in the biomarker protein NRP-1, (20) a receptor expressed on the outer plasma membrane of certain types of cancer cells, which is involved in angiogenesis, a hallmark of cancer growth, and tumor cell migration (21).…”

Section: Resultsmentioning

confidence: 99%

Quantitative ratiometric discrimination between noncancerous and cancerous prostate cells based on neuropilin-1 overexpression

Pallaoro

Braun

Moskovits

2011

Proc. Natl. Acad. Sci. U.S.A.

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A multiplexed, ratiometric method is described that can confidently distinguish between cancerous and noncancerous epithelial prostate cells in vitro. The technique is based on bright surfaceenhanced resonance Raman scattering (SERRS) biotags (SBTs) infused with unique Raman reporter molecules, and carrying cellspecific peptides. Two sets of SBTs were used. One targets the neuropilin-1 (NRP-1) receptors of cancer cells through the RPARPAR peptide. The other functions as a positive control (PC) and binds to both noncancerous and cancer cells through the HIV-derived TAT peptide. Point-by-point 2D Raman maps of the spatial distribution of the two tags were constructed with subcellular resolution from cells simultaneously incubated with the two sets of SBTs. Averaging the SERRS signal over a given cell yielded an NRP/PC ratio from which a robust quantitative measure of the overexpression of the NRP-1 by the cancer cell line was extracted. The use of a local, on-cell reference produces quantitative, statistically robust measures of overexpression independent of such sources of uncertainty as variations in the location of the focal plane, the local cell concentration, and turbidity.surface-enhanced Raman spectroscopy biomarker | cancer cell identification | multiplexing | silver nanoparticles E arly and rapid identification of malignant cells [ideally freeflowing in biological fluids such as urine (1) or blood (2-4)] is a central goal in cancer research. Accordingly, seeking improvements in sensitivity and accuracy of detection and quantification through, for example, the development of cell-specific diagnostic tools and biomarkers is an active enterprise. Although it is known that such cells are present in body fluids, concentrating them to levels appropriate for confident identification and quantification is still a serious challenge, despite significant advances that have been made by, for example, using microfluidics (5). Once collected, the cells must be identified as either cancerous or noncancerous within tolerable confidence limits, which may be improved by, for example, using several nonredundant biomarkers. Numerous promising identification methods have been reported using antibodies. In this article, we report a technique based on surface-enhanced Raman spectroscopy (SERS) and biotags that produce bright surface-enhanced resonance Raman scattering (SERRS) signals, comparable to or exceeding the intensities of fluorescent tags. The SERRS biotags (SBTs) used in this study exploit peptides as recognition moieties. We show that using SBTs ratiometrically can provide highly statistically significant, quantitative measures of neuropilin-1 (NRP-1) overexpression insensitive to normal causes of uncertainty in optical measurements such as variations in focal plane, cell concentration, and turbidity.Normal Raman signals from cells and their infrared (FTIR) absorbance patterns have been previously used to differentiate between cancer and normal cells (6-9). SERS has been used as an alternative immunohistochemistry (IH...

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“…The potential of CPPs to efficiently deliver cargo is dependent on the cellular association of the CPP to the target cell and the mechanism by which the CPP/cargo is transported into the cell. The mechanism of membrane translocation of CPPs and cargo, however, has yet to be identified definitively (Zorko and Langel 2005;Patel, Zaro et al 2007) and there are conflicting studies regarding whether the CPP internalization mechanism involves energy-dependent endocytosis or a non-endocytic mechanism (Drin, Cottin et al 2003;Richard, Melikov et al 2003;Ziegler, Nervi et al 2005). Despite the fact that different CPPs internalize into cells through different mechanisms (i.e., endocytosis or energy-independent membrane perturbations), recent observations have indicated that internalization of these CPPs occurs via endocytosis when the CPPs are coupled with high molecular weight cargo (Console, Marty et al 2003;Lundberg, Wikstrom et al 2003).…”

Section: Dicussionsmentioning

confidence: 99%

Evaluation of Cell-Penetrating Peptide/Adenovirus Particles for Transduction of CAR-Negative Cells

Nigatu

Vupputuri

Flynn

et al. 2013

Journal of Pharmaceutical Sciences

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Linear low‐density polyethylene (LLDPE), based on butene‐1 or hexene‐1, was irradiated with γ‐rays under vacuum or in the presence of air. The study focused on the influence of the dose rate and the γ‐dose on the thermal properties of LLDPE. Differential scanning calorimetry, thermogravimetric analysis (TGA), and TGA/FTIR techniques were used to address the thermal behavior as a result of γ‐irradiation. During this irradiation, competition between crosslinking and scission reactions, subsequent to oxidation reactions, occurred in the polymeric material, which strongly depends on the experimental conditions. A decrease of the crystallinity for γ‐irradiated samples was observed in particular for samples irradiated under vacuum. This observation may be explained by increased hindrance of segment mobility due to crosslinking reactions that prevent crystal growth. TGA investigations revealed an enhancement of the thermal stability for samples irradiated under vacuum but not for those irradiated in air. © 2006 Wiley Periodicals, Inc. J Appl Polym Sci 100: 2790–2795, 2006

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Cell-penetrating peptides: mechanism and kinetics of cargo delivery

Cited by 745 publications

References 87 publications

Identification of a Novel Cell-Penetrating Peptide from Human Phosphatidate Phosphatase LpIN3

Identification of a Novel Cell-Penetrating Peptide from Human Phosphatidate Phosphatase LpIN3

Quantitative ratiometric discrimination between noncancerous and cancerous prostate cells based on neuropilin-1 overexpression

Evaluation of Cell-Penetrating Peptide/Adenovirus Particles for Transduction of CAR-Negative Cells

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