Structural Variety of Membrane Permeable Peptides

Futaki, Shiroh; Goto, Susumu; Suzuki, Tadanao; Nakase, Ikuhiko; Sugiura, Yukio

doi:10.2174/1389203033487261

Cited by 58 publications

(55 citation statements)

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“…1B. Cationic peptide sequences derived from the HIV Tat protein 48 or other protein transduction domains (PTD) have been shown to promote cellular uptake of large molecules including nanocrystals 24 , and could be efficiently used as a cellular entry module. For delivery to specific cellular compartment, peptide recognition sequences (R in Fig.…”

Section: Modularity Of the Peptide Toolkitmentioning

confidence: 99%

Peptide-coated semiconductor nanocrystals for biomedical applications

et al. 2005

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We have developed a new functionalization approach for semiconductor nanocrystals based on a single-step exchange of surface ligands with custom-designed peptides. This peptide-coating technique yield small, monodisperse and very stable water-soluble NCs that remain bright and photostable. We have used this approach on several types of core and core-shell NCs in the visible and near-infrared spectrum range and used fluorescence correlation spectroscopy for rapid assessment of the colloidal and photophysical properties of the resulting particles. This peptide coating strategy has several advantages: it yields probes that are immediately biocompatible; it is amenable to improvements of the different properties (solubilization, functionalization, etc) via rational design, parallel synthesis, or molecular evolution; it permits the combination of several functions on individual NCs. These functionalized NCs have been used for diverse biomedical applications. Two are discussed here: single-particle tracking of membrane receptor in live cells and combined fluorescence and PET imaging of targeted delivery in live animals.

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Section: Modularity Of the Peptide Toolkitmentioning

confidence: 99%

Peptide-coated semiconductor nanocrystals for biomedical applications

et al. 2005

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“…Several AMPs are suggested to target bacterial components other than membranes such as nucleic acids. In recent years it became evident that a series of cationic antibacterial peptides can enter bacterial cells by passive transport (11). Buforin II and its truncated analogs penetrate the cell membrane but do not permeabilize it.…”

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confidence: 99%

Dermcidin-Derived Peptides Show a Different Mode of Action than the Cathelicidin LL-37 against Staphylococcus aureus

Senyürek

Paulmann

Sinnberg

et al. 2009

Antimicrob Agents Chemother

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Dermcidin (DCD) is an antimicrobial peptide which is constitutively expressed in eccrine sweat glands. By postsecretory proteolytic processing in sweat, the DCD protein gives rise to anionic and cationic DCD peptides with a broad spectrum of antimicrobial activity. Many antimicrobial peptides induce membrane permeabilization as part of their killing mechanism, which is accompanied by a loss of the bacterial membrane potential. In this study we show that there is a time-dependent bactericidal activity of anionic and cationic DCD-derived peptides which is followed by bacterial membrane depolarization. However, DCD-derived peptides do not induce pore formation in the membranes of gram-negative and gram-positive bacteria. This is in contrast to the mode of action of the cathelicidin LL-37. Interestingly, LL-37 as well as DCD-derived peptides inhibit bacterial macromolecular synthesis, especially RNA and protein synthesis, without binding to microbial DNA or RNA. Binding studies with components of the cell envelope of gram-positive and gram-negative bacteria and with model membranes indicated that DCD-derived peptides bind to the bacterial envelope but show only a weak binding to lipopolysaccharide (LPS) from gram-negative bacteria or to peptidoglycan, lipoteichoic acid, and wall teichoic acid, isolated from Staphylococcus aureus. In contrast, LL-37 binds strongly in a dosedependent fashion to these components. Altogether, these data indicate that the mode of action of DCD-derived peptides is different from that of the cathelicidin LL-37 and that components of the bacterial cell envelope play a role in the antimicrobial activity of DCD.

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“…Peptides derived from the third helix of the antennapedia homeodomain, herpes virus structural protein, and human immunodeficiency virus Tat protein have been used to deliver both small and large peptides of interest to the cells through an energy-and receptor-independent mechanism (12)(13)(14). Most of the PTD are arginine-rich peptides (15).…”

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confidence: 99%

Identification of a p65 Peptide That Selectively Inhibits NF-κ B Activation Induced by Various Inflammatory Stimuli and Its Role in Down-regulation of NF-κB-mediated Gene Expression and Up-regulation of Apoptosis

Takada

Singh²,

Aggarwal

2004

Journal of Biological Chemistry

170

130

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Because of the critical role of the nuclear transcription factor NF-B in inflammation, viral replication, carcinogenesis, antiapoptosis, invasion, and metastasis, specific inhibitors of this nuclear factor are being sought and tested as treatments. NF-B activation is known to require p65 phosphorylation at serine residues 276, 529, and 536 before it undergoes nuclear translocation. Small protein domains, termed protein transduction domains (PTDs), which are able to penetrate cell membranes can be used to transport other proteins across the cell membrane. We have identified two peptides from the p65 subunit of NF-B (P1 and P6 were from amino acid residues 271-282 and 525-537, respectively) that, when linked with a PTD derived from the third helix sequence of antennapedia, inhibited tumor necrosis factor (TNF)-induced NF-B activation in vivo. Linkage to the PTD was not, however, required to suppress the binding of the p50-p65-heterodimer to the DNA in vitro. PTD-p65-P1 had no effect on TNF-induced AP-1 activation. PTD-p65-P1 suppressed NF-B activation induced by lipopolysaccharide, interleukin-1, okadaic acid, phorbol 12-myristate 13-acetate, H 2 O 2 , and cigarette smoke condensate as well as that induced by TNF. PTD-p65-P1 had no effect on TNF-induced inhibitory subunit of NF-B (IB␣) phosphorylation, IB␣ degradation, or IB␣ kinase activation, but it blocked TNF-induced p65 phosphorylation and nuclear translocation. NF-B-regulated reporter gene expression induced by TNF, TNF receptor 1, TNF receptor-associated death domain, TNF receptor-associated factor-2, NF-B-inducing kinase, IB␣ kinase, and p65 was also suppressed by these peptides. Suppression of NF-B by PTD-p65-P1 enhanced the apoptosis induced by TNF and chemotherapeutic agents. Overall, our results demonstrate the identification of a p65 peptide that can selectively inhibit NF-B activation induced by various inflammatory stimuli, down-regulate NF-B-mediated gene expression, and up-regulate apoptosis.NF-B represents a group of five proteins, namely c-Rel, RelA (p65), RelB, NF-B1 (p50 and p105), and NF-B2 (p52) (1). Ways to modulate NF-B expression therapeutically have focused on its active-inactive state transition mechanisms. NF-B is regulated by a family of inhibitors, called IB 1 (2). In an inactive state, NF-B is present in the cytoplasm as a heterotrimer consisting of p50, p65, and IB␣ subunits. In response to an activation signal, the IB␣ subunit is phosphorylated at serine residues 32 and 36, ubiquitinated at lysine residues 21 and 22, and degraded through the proteosomal pathway, thus exposing the nuclear localization signals on the p50-p65 heterodimer. The p65 is then phosphorylated, leading to the nuclear translocation and binding to a specific sequence in DNA, which in turn results in transcriptions of various genes including cyclin D1, cyclooxygenase (COX)-2, and matrix metalloproteinase (MMP)-9.NF-B has been shown to regulate the expression of a number of genes whose products are involved in inflammation, viral replication, carcinogenesis, ant...

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Structural Variety of Membrane Permeable Peptides

Cited by 58 publications

References 0 publications

Peptide-coated semiconductor nanocrystals for biomedical applications

Peptide-coated semiconductor nanocrystals for biomedical applications

Dermcidin-Derived Peptides Show a Different Mode of Action than the Cathelicidin LL-37 against Staphylococcus aureus

Identification of a p65 Peptide That Selectively Inhibits NF-κ B Activation Induced by Various Inflammatory Stimuli and Its Role in Down-regulation of NF-κB-mediated Gene Expression and Up-regulation of Apoptosis

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