Disulfide bond formation in peptides by dimethyl sulfoxide. Scope and applications

Tam, James P.; Wu, Cui Rong; Li, Wen; Zhang, Jing Wen

doi:10.1021/ja00017a044

Cited by 504 publications

(414 citation statements)

References 3 publications

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“…However, at pH 6.6 the PHSM pop-upTAT released 60 wt.% of the initial DOX amount and at pH 6.4 (e.g., endosomal pH) the PHSM pop-upTAT released approximately 78 wt.% of the initial DOX amount. These pHsensitive DOX release properties of PHSM pop-upTAT are due to the physical destabilization of the hydrophobic core (resulting from ionization of polyHis) as the pH decreases [20][21][22][23][24][25]. In addition, DOX release behaviors of the PHSM or PHSM TAT with pH were similar to that of the PHSM pop-upTAT (data not shown).…”

Section: Ph-sensitivitymentioning

confidence: 86%

“…After freeze-drying, PLA(3kDa)-b-PEG (2kDa)-b-polyHis(2kDa)-Mal (yield: 80± 4 wt.%) was obtained. The DMSO-mediated oxidation of SH group to disulfide (-S-S-) may be occurred as a side reaction during the conjugation [22]. However, the addition of 6-fold excess Mal for SH group seemed to facilitate the chemical reaction between Mal-and SH-group.…”

Section: Synthesis Of Pla(3kda)-b-peg(2kda)-b-polyhis(2kda)-mal-mentioning

confidence: 99%

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Super pH-sensitive multifunctional polymeric micelle for tumor pHe specific TAT exposure and multidrug resistance

Lee

Gao

Kim

et al. 2008

Journal of Controlled Release

373

261

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As an alternative to cell specific cancer targeting strategies (which are often afflicted with the heterogeneity of cancer cells as with most biological systems), a novel polymeric micelle constitute of two block copolymers of poly(L-lactic acid)-b-poly(ethylene glycol)-b-poly(L-histidine)-TAT (transactivator of transcription) and poly(L-histidine)-b-poly(ethylene glycol) was developed. The micelle formed via the dialysis method was approximately 95 nm in diameter and contained 15 wt. % of doxorubicin (DOX) by weight. The micelle surface hides TAT during circulation, which has the strong capability to translocate the micelle into cells, and exposes TAT at a slightly acidic tumor extracellular pH to facilitate the internalization process. The micelle core was engineered for disintegration in early endosomal pH of tumor cells, quickly releasing DOX. The ionization process of the block copolymers and ionized polymers assisted in disrupting the endosomal membrane. This processes permitted high DOX concentrations in the cytosol and its target site of the nucleus, thus increasing DOX potency in various wild and multidrug resistant (MDR) cell lines (3.8-8.8 times lower IC 50 than free DOX, depending on cell line). When tested with the xenografted tumors of human ovarian tumor drug-resistant A2780/AD, human breast tumor drug-sensitive MCF-7, human lung tumor A549 and human epidermoid tumor KB in a nude mice model, all tumors significantly regressed in size by three bolus injections at a dose of DOX 10 mg equivalent/kg body per injection of DOX-loaded micelle at three day interval, while minimum weight loss was observed. This approach may replace the need for cell-specific antibodies or targeting ligands, thereby providing a general strategy for solid tumor targeting.

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Section: Ph-sensitivitymentioning

confidence: 86%

Section: Synthesis Of Pla(3kda)-b-peg(2kda)-b-polyhis(2kda)-mal-mentioning

confidence: 99%

Super pH-sensitive multifunctional polymeric micelle for tumor pHe specific TAT exposure and multidrug resistance

Lee

Gao

Kim

et al. 2008

Journal of Controlled Release

373

261

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“…For cecropin A it has been known for some time that the broad spectrum antibiotic activity decreased when the molecule was shortened by deletion of certain residues [8,19]. However, we recently reported several 26-residue ce- "Data from [13]. Table III shows that activity against S pyogenes increased by a factor of 20 when the hybrid was shortened from 26 to 20 residues.…”

Section: Discussionmentioning

confidence: 97%

“…PGL ", PYL" [10,11] and other antibiotical peptides from amphibian skin such as the magalnins [3] are smaller in size and thus less demanding synthetically [12], but somewhat less effective as antibiotics than the cecropins. Defensins [6], on the other hand, while showing interesting antibacterial, antifungal and antiviral properties, are rather complex, highly folded structures with three internal disulfide bonds and have so far proved rather difficult to prepare by chemical means [13]. We have recently reported that certain hybrids of cecropin A and melittin (M) show powerful antibacterial activities.…”

Section: Introductionmentioning

confidence: 99%

Shortened cecropin A‐melittin hybrids Significant size reduction retains potent antibiotic activity

et al. 1992

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We have earlier reported two 26‐residue antibacterial peptides made up from different segments ol'cecropin A (CA) and melittin (M). We now report a substantial reduction in size at the C‐terminal section of the highly active hybrid CA(1–8)M(1–18), leading to a series of 20‐, 18‐ and 15‐residue analogs with antibiotic properties similar to the larger molecule. In particular, the 15‐residue hybrids CA(1–7)M(2–9), CA(1–7)M(4–11) and CA(1–7)M(5–12) are the shortest cecropin‐based peptide antibiotics described so far, with antibacterial activity and spectra similar or better than cecropin A and a 60% reduction in size. Their reduced size and highly α‐helical structure require an alternative mechanism for their interaction with bacterial membranes.

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“…Peptides were dissolved in a small volume of dimethyl sulfoxide (DMSO) and diluted with water to 20% DMSO. Intermolecular disulfide bond formation of peptide A was performed by mild oxidation with 20% DMSO as described [19]. Peptide A was completely reduced by treatment with 1 mM DTT at 50°C for 15 min and subsequently alkylated by a 15-min incubation with 2.5 mM iodoacetamide (Sigma) at room temperature.…”

Section: Methodsmentioning

confidence: 99%

Modification of soybean sucrose synthase by S-thiolation with ENOD40 peptide A

Röhrig

John

Schmidt

2004

Biochemical and Biophysical Research Communications

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The gene ENOD40 is expressed at an early stage of root nodule organogenesis and has been postulated to play a central regulatory role in the Rhizobium-legume interaction. In vitro translation of soybean ENOD40 mRNA showed that the gene encodes two peptides of 12 and 24 aa residues (peptides A and B) that bind to sucrose synthase. Here we show that the small Cys-containing peptide A binds to sucrose synthase by disulfide bond formation, which may represent a novel form of posttranslational modification of this important metabolic enzyme. Assays using nanomolar concentrations of peptide A revealed that the monomeric reduced form of this peptide binds to purified sucrose synthase. Using a cysteinyl capture strategy combined with MALDI-TOF MS analysis we identified the Cys residue C264 of soybean sucrose synthase as the binding site of peptide A. Modification of sucrose synthase with ENOD40 peptide A activates sucrose cleavage activity whereas the synthesis activity of the enzyme is unaffected. The results are discussed in relation to the role of sucrose synthase in the control of sucrose utilization in nitrogen-fixing nodules. Ó 2004 Elsevier Inc. All rights reserved. The symbiotic interaction between leguminous plants and rhizobia results in the development of the nodule, a new organ on plant roots. In these nodules the bacteria are hosted intracellularly as bacteroids and find the ideal environment to fix atmospheric nitrogen. Nitrogen fixation is an energy-demanding process which is dependent on the supply of photosynthate. Sucrose, as the major end product of photosynthesis, is synthesized in leaves and is transported in the phloem to various sink tissues such as nodules. This disaccharide is cleaved by the homotetrameric enzyme sucrose synthase (SuSy) catalyzing the reversible, UDP-dependent cleavage of sucrose into UDP-glucose and fructose. This reaction is considered to function in vivo in the sucrose breakdown direction providing substrates for rapidly growing tissues and sink organs. SuSy is one of the most abundant proteins in mature legume nodules [1,2], and breakdown of sucrose is a key step in nitrogen fixation and a necessary prerequisite for normal nodule development and function [3].Due to the important role of SuSy in the control of sucrose utilization in sink tissues, the expression of SuSy genes is highly regulated on the transcriptional and translational levels [4]. Moreover, SuSy is posttranslationally modified by reversible protein phosphorylation [5,6], and the soluble form of SuSy can bind to the actin cytoskeleton in plants [7]. Recently, we reported direct binding of SuSy to peptide A (12 aa residues) and peptide B (24 aa residues) encoded by the early nodulin gene ENOD40 [8]. In addition to the two small peptides, the secondary structure of ENOD40 mRNA has been shown to be a key element in the signaling process underlying nodule organogenesis [9,10].

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Disulfide bond formation in peptides by dimethyl sulfoxide. Scope and applications

Cited by 504 publications

References 3 publications

Super pH-sensitive multifunctional polymeric micelle for tumor pHe specific TAT exposure and multidrug resistance

Super pH-sensitive multifunctional polymeric micelle for tumor pHe specific TAT exposure and multidrug resistance

Shortened cecropin A‐melittin hybrids Significant size reduction retains potent antibiotic activity

Modification of soybean sucrose synthase by S-thiolation with ENOD40 peptide A

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