Predicting cell-penetrating peptides

Hansen, Mats; Kilk, Kalle; Langel, Ülo

doi:10.1016/j.addr.2007.09.003

Cited by 148 publications

(117 citation statements)

References 53 publications

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“…Thus, the presence of carbohydrate(s) decrease the capacity of the glycosylated CPP cargo conjugate to enter cells, in contrast to serine or threonine residues. This conclusion applies even though (Arg) 6 is still efficiently taken up into cells [50,51], and the glycosylated CPPs reported here have six arginines in their sequences.…”

Section: Fluorescence Labeling Of Cho-k1 Cells Incubated With Klak 3supporting

confidence: 61%

“…After filtration, the filtrate was concentrated to give an oil, which was purified by column chromatography on silica gel (EtOAc/MeOH 9:1) to give 315. 6 To a solution of 3-azidopropyl-β-D-galactopyranoside 5 (157.8 mg, 0.60 mmol) in anhydrous pyridine (2.5 mL) was added acetic anhydride (395 µL, 4.20 mmol, 7 eq.) under argon.…”

Section: -Azidopropyl-β-d-galactopyranosidementioning

confidence: 99%

“…Today, plethora of basic peptides which correspond to segments of natural proteins, synthetic peptides, or platforms have been described and are classified as cellpenetrating peptides (CPPs) [3][4][5][6]. It has also been demonstrated that CPPs have the capacity to shuttle bioactive cargoes inside eukaryotic cells.…”

Section: Introductionmentioning

confidence: 99%

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Glycosylated cell-penetrating peptides and their conjugates to a proapoptotic peptide: preparation by click chemistry and cell viability studies

et al. 2009

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Cell-penetrating peptides (CPPs), which are usually short basic peptides, are able to cross cell membranes and convey bioactive cargoes inside cells. CPPs have been widely used to deliver inside cells peptides, proteins, and oligonucleotides; however, their entry mechanisms still remain controversial. A major problem concerning CPPs remains their lack of selectivity to target a specific type of cell and/or an intracellular component. We have previously shown that myristoylation of one of these CPPs affected the intracellular distribution of the cargo. We report here on the synthesis of glycosylated analogs of the cell-penetrating peptide (R6/W3): Ac-RRWWRRWRR-NH 2 . One, two, or three galactose(s), with or without a spacer, were introduced into the sequence of this nonapeptide via a triazole link, the Huisgen reaction being achieved on a solid support. Four of these glycosylated CPPs were coupled via a disulfide bridge to the proapoptotic KLAK peptide, (KLAKLAKKLAKLAK), which alone does not enter into cells. The effect on cell viability and the uptake efficiency of different glycosylated conjugates were studied on CHO cells and were compared to those of the nonglycosylated conjugates: (R6/W3)S-S-KLAK and penetratinS-S-KLAK. We show that glycosylation significantly increases the cell viability of CHO cells compared to the nonglycosylated conjugates and concomitantly decreases the internalization of the KLAK cargo. These results suggest that glycosylation of CPP may be a key point in targeting specific cells.

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Section: Fluorescence Labeling Of Cho-k1 Cells Incubated With Klak 3supporting

confidence: 61%

Section: -Azidopropyl-β-d-galactopyranosidementioning

confidence: 99%

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Glycosylated cell-penetrating peptides and their conjugates to a proapoptotic peptide: preparation by click chemistry and cell viability studies

et al. 2009

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“…Since the initial evidence that antennapedia homeobox (1)(2)(3) protein can cross cell membranes came to light, numerous peptides with similar internalization properties have been described (4). These cell-penetrating peptides are more or less amphipathic peptides generally rich in lysyl and arginyl residues.…”

mentioning

confidence: 99%

Cell-penetrating Peptides with Intracellular Actin-remodeling Activity in Malignant Fibroblasts

Delaroche

Cantrelle

Subra

et al. 2010

Journal of Biological Chemistry

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Cell-penetrating peptides can cross cell membranes and are commonly seen as biologically inert molecules. However, we found that some cell-penetrating peptides could remodel actin cytoskeleton in oncogene-transformed NIH3T3/EWS-Fli cells. These cells have profound actin disorganization related to their tumoral transformation. These arginine-and/or tryptophanrich peptides could cross cell membrane and induce stress fiber formation in these malignant cells, whereas they had no perceptible effect in non-tumoral fibroblasts. In addition, motility (migration speed, random motility coefficient, wound healing) of the tumor cells could be decreased by the cell-permeant peptides. Although the peptides differently influenced actin polymerization in vitro, they could directly bind monomeric actin as determined by NMR and calorimetry studies. Therefore, cellpenetrating peptides might interact with intracellular protein partners, such as actin. In addition, the fact that they could reverse the tumoral phenotype is of interest for therapeutic purposes.

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“…It is one of the well-studied cell-penetrating peptides. Tat is a group of short peptides sharing the ability of translocation across several biological membranes and can also carry various macromolecular cargoes such as proteins, antibodies, toxins, oligonucleotides, DNA, imaging agents and nanoparticles through membranes without affecting the activity of the cargoes (Gupta et al, 2005;Hansen et al, 2008;Fonseca et al, 2009;Koren et al, 2011). In this present study, the physical properties, chemical stability and hypoglycemic activity of the insulin-Tat mixture loaded in niosomes were investigated and evaluated for the oral delivery efficacy of this mixture.…”

Section: Introductionmentioning

confidence: 99%

Hypoglycemic activity and stability enhancement of human insulin–tat mixture loaded in elastic anionic niosomes

et al. 2016

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This study aimed to investigate the synergistic effect of trans-activator of transcription (Tat) and niosomes for the improvement of hypoglycemic activity of orally delivered human insulin. The elastic anionic niosomes composing of Tween 61/cholesterol/dicetyl phosphate/sodium cholate at 1:1:0.05:0.02 molar ratio loaded with insulin-Tat mixture (1:3 molar ratio) was prepared. Deformability of the elastic anionic niosomes decreased after loaded with the mixture of 1.35 times. For the in vitro release, the insulin (T 10 ¼ 4 h) loaded in the elastic anionic niosomes indicated the slower release rate than insulin in the mixture (T 10 ¼ 3 h) loaded in niosomes. At room temperature (30 ± 2 C), the mixture loaded in elastic anionic niosomes was more chemical stable than the free mixture of 1.3, 1.4 and 1.7 times after stored for 4, 8 and 12 weeks, respectively. Oral administration in the alloxan-induced diabetic mice of the mixture loaded in elastic anionic niosomes with the insulin doses at 25, 50 and 100 IU/kg body weight indicated significant hypoglycemic activity with the percentage fasting blood glucose reduction of 1.95, 2.10 and 2.10 folds of the subcutaneous insulin injection at 12 h, respectively. This study has demonstrated the synergistic benefits of Tat and elastic anionic niosomes for improving the hypoglycemic activity of the orally delivered human insulin as well as the stability enhancement of human insulin when stored at high temperature. The results from this study can be further developed as an effective oral insulin delivery.

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Predicting cell-penetrating peptides

Cited by 148 publications

References 53 publications

Glycosylated cell-penetrating peptides and their conjugates to a proapoptotic peptide: preparation by click chemistry and cell viability studies

Glycosylated cell-penetrating peptides and their conjugates to a proapoptotic peptide: preparation by click chemistry and cell viability studies

Cell-penetrating Peptides with Intracellular Actin-remodeling Activity in Malignant Fibroblasts

Hypoglycemic activity and stability enhancement of human insulin–tat mixture loaded in elastic anionic niosomes

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