Small Efficient Cell-penetrating Peptides Derived from Scorpion Toxin Maurocalcine

Poillot, Cathy; Bichraoui, Hicham; Tisseyre, Céline; Bahemberae, Eloi; Andreotti, Nicolas; Sabatier, Jean‐Marc; Ronjat, Michel; Waard, Michel De

doi:10.1074/jbc.m112.360628

Cited by 25 publications

(34 citation statements)

References 24 publications

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“…In contrast, our findings herein demonstrated that TAT is unnecessary for NoxA1ds to cross cell membranes, and we attribute this in part to the positively charged lysines in the C terminus of NoxA1ds and the alternating hydrophobic/hydrophilic amino acid structure of NoxA1ds. Indeed, other short peptides with similar hydropathy patterns have proven highly cell permeant and thus support our findings (50).…”

Section: Epvd(y3 A)-lgkakv 205supporting

confidence: 88%

“…Notwithstanding the broadly demonstrated effectiveness of related peptides by parenteral, peritoneal, subcutaneous, and direct application to blood vessels using gene therapy (46,50), the limitations in the use of peptides as "druggable" therapeutics are obvious. These include a very limited oral bioavailability due to peptide degradation in the gut.…”

Section: Journal Of Biological Chemistrymentioning

confidence: 99%

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Selective Recapitulation of Conserved and Nonconserved Regions of Putative NOXA1 Protein Activation Domain Confers Isoform-specific Inhibition of Nox1 Oxidase and Attenuation of Endothelial Cell Migration

Ranayhossaini

Rodríguez

Sahoo

et al. 2013

Journal of Biological Chemistry

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Background: Nox1, an oxidant source in colon carcinoma and vascular disease, is activated by NOXA1. Results: A NOXA1 peptide blocked NOXA1-Nox1 binding and inhibited colon carcinoma and endothelial oxidants and migration. Conclusion:The findings identify a NOXA1-activating domain and an isoform-specific Nox1 inhibitor. Significance: The data provide insight into Nox1 regulation and present a potential therapy for suppressing oxidative stressrelated disease.

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Section: Epvd(y3 A)-lgkakv 205supporting

confidence: 88%

Section: Journal Of Biological Chemistrymentioning

confidence: 99%

Selective Recapitulation of Conserved and Nonconserved Regions of Putative NOXA1 Protein Activation Domain Confers Isoform-specific Inhibition of Nox1 Oxidase and Attenuation of Endothelial Cell Migration

Ranayhossaini

Rodríguez

Sahoo

et al. 2013

Journal of Biological Chemistry

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“…The chemical synthesis of Tyr-L-MCa and the folding / oxidation process were not affected by the extra tyrosine residue added to the N-terminal end of the peptide. These results together with previous observations of the Brought to you by | New York University Bobst Library Technical Services Authenticated Download Date | 6/1/15 1:15 PM great tolerance in sequence variation with respect to the cell penetrating properties of MCa [28,29] strongly suggest that Tyr-L-MCa should retain its native properties. The position of the extra tyrosine residue ensures that iodination occurs in a convenient way, without accessibility problems and modification of the native sequence.…”

Section: Discussionsupporting

confidence: 76%

Selective mono-radioiodination and characterization of a Cell-Penetrating Peptide: L-Tyr-Maurocalcine

Ahmadi¹,

Bacot²,

Poillot³

et al. 2014

Radiochimica Acta

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Mono-and poly-iodinated peptides form frequently during radioiodination procedures. However, the formation of a single species in its mono-iodinated form is essential for quantitative studies such as determination of tissue concentration or image quantification. Therefore, the aim of the present study was to define the optimal experimental conditions in order to exclusively obtain the mono-iodinated form of L-maurocalcine (L-MCa). L-MCa is an animal venom toxin which was shown to act as a cellpenetrating peptide. In order to apply the current direct radioiodination technique using oxidative agents including chloramine T, Iodo-Gen ® or lactoperoxidase, an analogue of this peptide containing a tyrosine residue (Tyr-L-MCa) was synthesized and was shown to fold/oxidize properly.The enzymatic approach using lactoperoxidase/H 2 O 2 was found to be the best method for radioiodination of Tyr-LMCa. MALDI-TOF mass spectrometry analyses were then used for identification of the chromatographic eluting components of the reaction mixtures. We observed that the production of different radioiodinated species depended upon the reaction conditions. Our results successfully described the experimental conditions of peptide radioiodination allowing the exclusive production of the mono-iodinated form with high radiochemical purity and without the need for a purification step. Mono-radioiodination of L-Tyr-MCa will be crucial for future quantitative studies, investigating the mechanism of cell penetration and in vivo biodistribution.

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“…35 Hence, the reason for the lack of internalization of the peptide in our studies, especially in the cancer cells, is not clear. Maurocalcine is a highly potent CPP.…”

Section: Cpp-dy676 Conjugates Into Cancer and Noncancer Cellsmentioning

confidence: 71%

New generation CPPs show distinct selectivity for cancer and noncancer cells

Tansi

Filatova

Koroev

et al. 2018

J of Cellular Biochemistry

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In the last three decades, many new cell‐penetrating peptides (CPPs) were developed that exhibited enhanced cell selectivity. Thus, we aimed to validate the tumor cell selectivity of peptides from this new generation, namely fragments mini‐crotamine and mini‐maurocalcine. Both of these peptides are derived from venoms. Furthermore, we studied an analog of the classical CPP HIV‐TAT(47‐57) with alternating chirality of Arg residues. To allow covalent coupling of cargoes or fluorophores, a cysteine residue was introduced to the N‐terminus of the synthesized peptides. The therapeutic antibody trastuzumab conjugated to different fluorescent dyes was used for internalization studies. Comparison of uptake efficiencies revealed that CPPs of the new generation are in contrast to MPG‐peptides, nearly unable to internalize the noncovalently formed complexes with trastuzumab. Interestingly, the fluorescent derivative of the crotamine fragment was mainly observed in a subpopulation of breast cancer cells, whereas it was homogenously distributed in fibrosarcoma, colon cancer, and noncancerous endothelia cells. Thus, the fluorescent crotamine fragment reported herein is a potent theranostic tool for image‐guided applications. This peptide can be used to pinpoint the level of heterogeneity present within tumors and aid in the generation of therapeutics that target heterogenic subpopulations.

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Small Efficient Cell-penetrating Peptides Derived from Scorpion Toxin Maurocalcine

Cited by 25 publications

References 24 publications

Selective Recapitulation of Conserved and Nonconserved Regions of Putative NOXA1 Protein Activation Domain Confers Isoform-specific Inhibition of Nox1 Oxidase and Attenuation of Endothelial Cell Migration

Selective Recapitulation of Conserved and Nonconserved Regions of Putative NOXA1 Protein Activation Domain Confers Isoform-specific Inhibition of Nox1 Oxidase and Attenuation of Endothelial Cell Migration

Selective mono-radioiodination and characterization of a Cell-Penetrating Peptide: L-Tyr-Maurocalcine

New generation CPPs show distinct selectivity for cancer and noncancer cells

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