Arginine-rich intracellular delivery peptides noncovalently transport protein into living cells

Wang, Yahui; Chen, Chung‐Pin; Chan, Ming‐Huan; Chang, Mei‐Chi; Hou, Yu-Wun; Chen, Hwei-Hsien; Hsu, Hui-Ru; Liu, Kevin; Lee, Han-Jung

doi:10.1016/j.bbrc.2006.05.205

Cited by 64 publications

(73 citation statements)

References 30 publications

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“…However, the exact mechanism by which PTDs can promote the penetration of a peptide into the skin and other tissues is still unclear [3,4]. Although in this study we did not investigate the mechanisms by which covalently attached or non-attached PTDs can promote the penetration of peptides into viable layers of the skin, some speculation can be made.…”

Section: Resultsmentioning

confidence: 63%

“…To date, most studies used PTDs covalently attached to the therapeutic peptide, which results in increased synthesis costs and limitations for the use of these carriers. Recently, Wang et al [4] questioned the requirement of covalent linkage by showing that several arginine-rich intracellular delivery (AID) peptides not covalently attached to model proteins can promote the entry of the model protein into living cells in vitro and into mouse skin in vivo.…”

Section: Introductionmentioning

confidence: 99%

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Enhanced skin penetration of P20 phosphopeptide using protein transduction domains

Lopes

Furnish

Komalavilas

et al. 2008

European Journal of Pharmaceutics and Biopharmaceutics

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Protein transduction domains (PTDs) were recently demonstrated to increase the penetration of the model peptide P20 when the PTD and P20 were covalently attached. Here, we evaluated whether non-covalently linked PTDs were capable of increasing the skin penetration of P20. Two different PTDs were studied: YARA and WLR. Porcine ear skin mounted in a Franz diffusion cell was used to assess the penetration of P20 in the stratum corneum (SC) and viable skin (VS); VS consists of dermis and epidermis without SC. The transdermal delivery of P20 was also assessed. At 1 mM, YARA promoted a 2.33-fold increase in the retention of P20 in the SC but did not significantly increase the amount of P20 that reached VS. WLR significantly increased (2.88-fold) the penetration of P20 in VS. Compared to the non-attached form, the covalently linked WLR fragment was two times more effective in promoting the penetration of P20 into VS. None of the PTDs promoted transdermal delivery of P20 at 4 h post-application. It was concluded that selected non-covalently linked PTDs can be used as a penetration enhancer, but greater skin penetration efficiency can be achieved by covalently binding the PTD to the therapeutic agent.

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Section: Resultsmentioning

confidence: 63%

Section: Introductionmentioning

confidence: 99%

Enhanced skin penetration of P20 phosphopeptide using protein transduction domains

Lopes

Furnish

Komalavilas

et al. 2008

European Journal of Pharmaceutics and Biopharmaceutics

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“…The increase in local concentration of the Tatbound cargo at the cell surface results in cellular entry via endocytosis (Brooks et al, 2005). The non-covalent conjugate of CPPs and cargo protein and its effect on transduction has been also reported (Wang et al, 2006;Chen et al, 2007;Hu et al, 2009). The higher enhancement of cellular GFP uptake by Tat than V peptide might be due to the higher number of positively charged amino acids of Tat which is needed to facilitate the delivery of large proteins (Furuhata et al, 2006).…”

Section: Discussionmentioning

confidence: 79%

Polioviral receptor binding ligand: A novel and safe peptide drug carrier from polioviral capsid

Manosroi¹,

Lohcharoenkal²,

Götz³

et al. 2011

Drug Delivery

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“…cyclosporine, doxorubicin) to siRNAs and macromolecules (proteins, plasmids and liposomes) (118)(119)(120)(121). PTDs can be either covalently attached to the cargos or could form noncovalent complexes with them (122)(123)(124) (Table III).…”

Section: Ptd Technologymentioning

confidence: 98%

Transduction of Human Recombinant Proteins into Mitochondria as a Protein Therapeutic Approach for Mitochondrial Disorders

Papadopoulou

Tsiftsoglou

2011

Pharm Res

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Protein therapy is considered an alternative approach to gene therapy for treatment of genetic-metabolic disorders. Human protein therapeutics (PTs), developed via recombinant DNA technology and used for the treatment of these illnesses, act upon membrane-bound receptors to achieve their pharmacological response. On the contrary, proteins that normally act inside the cells cannot be developed as PTs in the conventional way, since they are not able to "cross" the plasma membrane. Furthermore, in mitochondrial disorders, attributed either to depleted or malfunctioned mitochondrial proteins, PTs should also have to reach the subcellular mitochondria to exert their therapeutic potential. Nowadays, there is no effective therapy for mitochondrial disorders. The development of PTs, however, via the Protein Transduction Domain (PTD) technology offered new opportunities for the deliberate delivery of human recombinant proteins inside eukaryotic subcellular organelles. To this end, mitochondrial disorders could be clinically encountered with the delivery of human mitochondrial proteins (engineered via recombinant DNA and PTD technologies) at specific intramitochondrial sites to exert their function. Overall, PTD-mediated Protein Replacement Therapy emerges as a suitable model system for the therapeutic approach for mitochondrial disorders.

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Arginine-rich intracellular delivery peptides noncovalently transport protein into living cells

Cited by 64 publications

References 30 publications

Enhanced skin penetration of P20 phosphopeptide using protein transduction domains

Enhanced skin penetration of P20 phosphopeptide using protein transduction domains

Polioviral receptor binding ligand: A novel and safe peptide drug carrier from polioviral capsid

Transduction of Human Recombinant Proteins into Mitochondria as a Protein Therapeutic Approach for Mitochondrial Disorders

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