Translocation of Analogues of the Antimicrobial Peptides Magainin and Buforin across Human Cell Membranes

Takeshima, Kenta; Chikushi, Akinori; Lee, Kyung-Kwon; Yonehara, Shin; Matsuzaki, Katsumi

doi:10.1074/jbc.m208762200

Cited by 185 publications

(159 citation statements)

References 42 publications

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“…The common mode of action of antimicrobial peptides is disruption of bacterial cell membranes via electrostatic and hydrophobic interactions [1,3,4,12,14,[29][30][31][32][33][34][35][36]. It is believed that amphipatic peptides can penetrate or form pores in the cell membranes through the insertion into the lipid bilayer mediated by hydrophobic forces, while their electrostatic interaction with phospholipid headgroups leads to membrane disruption.…”

Section: Factors Governing Bioactivity Of Camel-smentioning

confidence: 99%

Application of ‘Inductive’ QSAR Descriptors for Quantification of Antibacterial Activity of Cationic Polypeptides

Cherkasov

Jankovic²

2004

Molecules

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Abstract:On the basis of the inductive QSAR descriptors we have created a neural network-based solution enabling quantification of antibacterial activity in the series of 101 synthetic cationic polypeptides (CAMEL-s). The developed QSAR model allowed 80% correct categorical classification of antibacterial potencies of the CAMEL-s both in the training and the validation sets. The accuracy of the activity predictions demonstrates that a narrow set of 3D sensitive 'inductive' descriptors can adequately describe the aspects of intra-and intermolecular interactions that are relevant for antibacterial activity of the cationic polypeptides. The developed approach can be further expanded for the larger sets of biologically active peptides and can serve as a useful quantitative tool for rational antibiotic design and discovery.

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Section: Factors Governing Bioactivity Of Camel-smentioning

confidence: 99%

Application of ‘Inductive’ QSAR Descriptors for Quantification of Antibacterial Activity of Cationic Polypeptides

Cherkasov

Jankovic²

2004

Molecules

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“…On one hand, antimicrobial peptides are taken up into mammalian cells (15), and on the other hand CPPs show antimicrobial activity (16). Therefore, we considered whether a lactoferricin-derived peptide would also have the ability to act as a CPP by entering into mammalian cells.…”

mentioning

confidence: 99%

A Cell-penetrating Peptide Derived from Human Lactoferrin with Conformation-dependent Uptake Efficiency

Duchardt

Ruttekolk

Verdurmen

et al. 2009

Journal of Biological Chemistry

112

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The molecular events that contribute to the cellular uptake of cell-penetrating peptides (CPP) are still a matter of intense research. Here, we report on the identification and characterization of a 22-amino acid CPP derived from the human milk protein, lactoferrin. The peptide exhibits a conformation-dependent uptake efficiency that is correlated with efficient binding to heparan sulfate and lipid-induced conformational changes. The peptide contains a disulfide bridge formed by terminal cysteine residues. At concentrations exceeding 10 M, this peptide undergoes the same rapid entry into the cytoplasm that was described previously for the arginine-rich CPPs nona-arginine and Tat. Cytoplasmic entry strictly depends on the presence of the disulfide bridge. To better understand this conformation dependence, NMR spectroscopy was performed for the free peptide, and CD measurements were performed for free and lipidbound peptide. In solution, the peptides showed only slight differences in secondary structure, with a predominantly disordered structure both in the presence and absence of the disulfide bridge. In contrast, in complex with large unilamellar vesicles, the conformation of the oxidized and reduced forms of the peptide clearly differed. Moreover, surface plasmon resonance experiments showed that the oxidized form binds to heparan sulfate with a considerably higher affinity than the reduced form. Consistently, membrane binding and cellular uptake of the peptide were reduced when heparan sulfate chains were removed.

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“…The membrane permeability is dependent on the -helical content of the peptides (Park et al, 2000). Although it efficiently translocates into HeLa cells (Takeshima et al, 2003), it cannot penetrate ES cells whether the 6xHis-tag is located N-terminally or C-terminally (Fig. 3).…”

Section: Delivery Of Functional Proteinsmentioning

confidence: 99%

“…The translocational efficiency of a CPP depends on the amino acid sequence and the length of the CPP. Buforin 2 is a 21-residue peptide containing a +7 net charge (TRSSRAGLQFPVGRVHRLLRK) and is a membrane-permeabilizing antimicrobial peptide (Takeshima et al, 2003). Its structure is amphipathic, consisting of an N-terminal random coil region, an extended helical region, a hinge, and a C-terminal regular -helical region.…”

Section: Delivery Of Functional Proteinsmentioning

confidence: 99%

Embryonic Stem Cells: Introducing Exogenous Regulators into Embryonic Stem Cells

Cheon¹

2011

Embryonic Stem Cells - Basic Biology to Bioengineering

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Translocation of Analogues of the Antimicrobial Peptides Magainin and Buforin across Human Cell Membranes

Cited by 185 publications

References 42 publications

Application of ‘Inductive’ QSAR Descriptors for Quantification of Antibacterial Activity of Cationic Polypeptides

Application of ‘Inductive’ QSAR Descriptors for Quantification of Antibacterial Activity of Cationic Polypeptides

A Cell-penetrating Peptide Derived from Human Lactoferrin with Conformation-dependent Uptake Efficiency

Embryonic Stem Cells: Introducing Exogenous Regulators into Embryonic Stem Cells

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