Purification and pore-forming activity of two hydrophobic polypeptides from the secretion of the Red Sea Moses sole (Pardachirus marmoratus).

Lazarovici, Philip; Primor, Naftali; Loew, Leslie M.

doi:10.1016/s0021-9258(18)66622-0

Cited by 139 publications

(20 citation statements)

References 39 publications

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“…Structurally, the main constituent of the Lipo-Par, phospholipid DSEP-PEG 2000 -NH 2 , is covalently bound to the cationic peptide pardaxin by a condensation reaction. Pardaxin, also known as GE33, is a 33-amino-acid cationic antimicrobial peptide derived from the Red Sea Moses sole Pardachirus marmoratus that has hydrophobic and pore-forming properties − and can insert into phospholipid bilayers, rapidly localize to the ER through a nonlysosomal intracellular transport pathway, and cause an ER stress response . We hypothesized that cationic liposomes modified with pardaxin can utilize cell internalization and intracellular transport mechanisms similar to those of SV40 and similarly localize to the ER.…”

Section: Introductionmentioning

confidence: 99%

Virus-like Nonvirus Cationic Liposome for Efficient Gene Delivery via Endoplasmic Reticulum Pathway

et al. 2020

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Gene vectors play a critical role in gene therapy. To achieve efficient transfection, we developed a novel nonvirus cationic liposome (Lipo-Par), which was bound covalently with the cationic polypeptide pardaxin (Par). Interestingly, the Lipo-Pars exhibited highly enhanced gene transfection efficiency in various cell lines compared to that of the non-Par-bonded liposomes (Lipo-Nons). As a result, the internalization and intracellular transport mechanisms of the Lipo-Pars were investigated, and the findings indicated their ability to actively target the endoplasmic reticulum (ER) by moving along the cell cytoskeleton after undergoing caveolin-mediated endocytosis. This intracellular transport process is similar to that of some viruses. It was also found that ER stress and calcium level disturbances can affect the Lipo-Par-mediated expression of certain exogenous genes. A possible, yet non-negligible explanation for the high transfection efficiency of the Lipo-Par is its virus-like intracellular behavior and the intimate relationship between the ER membrane and the nuclear envelope.

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Section: Introductionmentioning

confidence: 99%

Virus-like Nonvirus Cationic Liposome for Efficient Gene Delivery via Endoplasmic Reticulum Pathway

et al. 2020

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“…Pardaxin is an amphipathic neurotoxin peptide composed of 33 amino acids (GFFALIPKIISSPLFKTLLSAVGSALSSSGGQE) that is classified as an AMP. It was initially isolated from the Red Sea Moses sole, Pardachirus marmoratus. The structure of Pardaxin is a helix–hinge–helix, which is a common structural motif found in both AMPs and cytotoxic peptides . In general, Pardaxin is composed of two structural D1 and D2 domains.…”

Section: Introductionmentioning

confidence: 99%

Identification of the Crucial Residues in the Early Insertion of Pardaxin into Different Phospholipid Bilayers

Jafari

Mehrnejad

Aghdami

et al. 2017

J. Chem. Inf. Model.

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Antimicrobial peptides (AMPs) are part of the innate host defense system, and they are produced by living organisms to defend themselves against infections. Pardaxin is a cationic AMP with antimicrobial and antitumor activities that has potential to be used as a novel antibiotic or for drug delivery in cancer therapy. This peptide acts on the membrane of target cells and can lead to lysis using different mechanisms of action. Here, we conducted 4.5 μs all-atom molecular dynamics (MD) simulations to determine the critical fragments and residues of Pardaxin for early insertion into different lipid bilayers. Our results revealed that the N-terminal domain of the peptide, particularly the Phe 2 and (/or) Phe 3 residues, has a crucial role in early insertion, independent of the type of lipid bilayers.

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“…It was particularly notable that with these spectral fingerprints, SFG-VS is able to unambiguously differentiate the interfacial random-coil (or loop) and α-helical structures in proteins. , One can thus naturally anticipate that such ability could enable the direct observation of the early steps of folding and the dynamics of α-helical formation within membrane environments. It is known that the membrane protein folding processes can be regulated by the membrane parameters such as the lipid chain length, fluidity, and headgroup charge. − Some studies suggested that the presence of negatively charged lipid in zwitterionic phosphatidylcholine (PC) membrane can induce a higher level of α-helicity of peptides, while other studies claimed the introduction of the anionic phosphatidylglycerol (PG) into the PC vesicles can cause a loss in α-helicity . But the underlying mechanism at the molecular level is unclear.…”

Section: Introductionmentioning

confidence: 99%

Amide III SFG Signals as a Sensitive Probe of Protein Folding at Cell Membrane Surface

Huang

Tian

et al. 2016

J. Phys. Chem. C

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A good understanding of membrane protein folding at the molecular level requires an effective means to determine the dynamical structural changes on coil-to-helix transition within cell membrane, yet remains challenging. Herein, we demonstrate that the amide III spectral signals of protein backbone, generated in the sum frequency generation vibrational spectroscopy, are a powerful tool to probe the protein folding processes within the membrane in situ, in real time and without exogenous labels. The amide III signals are capable of separating the spectral profiles of the random-coil and α-helical structures at the interface. The intensity ratio of coil and helix peaks becomes a prime indicator that allows to directly capturing the dynamical change of the coil-helix transition. With this approach, using pardaxin as model, the influence of lipid charge on the peptide folding degree at cell membrane surface has been nicely elucidated. It is evident that negative charge of lipid increases the folding degree of pardaxin upon interfacial adsorption and promotes the formation of α-helical structure during the insertion of peptide into lipid bilayer. This robust spectral approach can thus greatly enhance our ability to monitor the dynamics of membrane proteins in a real cell environment in situ.

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Purification and pore-forming activity of two hydrophobic polypeptides from the secretion of the Red Sea Moses sole (Pardachirus marmoratus).

Cited by 139 publications

References 39 publications

Virus-like Nonvirus Cationic Liposome for Efficient Gene Delivery via Endoplasmic Reticulum Pathway

Virus-like Nonvirus Cationic Liposome for Efficient Gene Delivery via Endoplasmic Reticulum Pathway

Identification of the Crucial Residues in the Early Insertion of Pardaxin into Different Phospholipid Bilayers

Amide III SFG Signals as a Sensitive Probe of Protein Folding at Cell Membrane Surface

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