Category: 79642-50-5

On July 15, 2020, Lei, Yanli; Wu, Miaosen; Wang, Junyi; Zhang, Hongtao; Zhan, Xiaobei; Sun, Zhenglong; Wu, Jianrong published an article.Name: Bis(2,5-dioxopyrrolidin-1-yl) glutarate The title of the article was Preparation and property of a biantenna macromolecule based on polysialic acid. And the article contained the following:

Polysialic acid (PSA), an acidic polysaccharide usually exists as a double-chain structure on cell adhesion mols. in vertebrates. The available PSA produced from Escherichia coli fermentation, however, is monochain PSA. In this work, a biomimetic biantenna type PSA (biPSA) was synthesized in vitro under mild conditions, and the terminal nonreducing ends of sialic acid residue were retained. The structure of biPSA was characterized through IR spectroscopy, and NMR, and the double-chain structure of biPSA was confirmed by the doubled mol. weight and particle size of biPSA. Anal. through CD, isothermal titration calorimetry, and thermostability experiments revealed that the obtained biPSA was more stable in aqueous solution than PSA, especially after complexation with Ca2+, which increased the variation in enthalpy and entropy. However, the addition of Cu2+ had a negligible effect on configuration of PSA and biPSA. The addition of Ca2+ promoted cell proliferation in a culture of microglia BV-2 cells with biPSA in medium. By contrast, the addition of Cu2+ had toxic effects. Supplementation with biPSA can maintain cell viability for a longer period than supplementation with monochain PSA. This work indicates that biPSA is a potential substitute for monochain PSA in practical applications. The experimental process involved the reaction of Bis(2,5-dioxopyrrolidin-1-yl) glutarate(cas: 79642-50-5).Name: Bis(2,5-dioxopyrrolidin-1-yl) glutarate

The Article related to biantenna macromol polysialic acid, biantenna structure, biomimetic macromolecule, ncam, polysialic acid, Placeholder for records without volume info and other aspects.Name: Bis(2,5-dioxopyrrolidin-1-yl) glutarate

Referemce:
Ester – Wikipedia,
Ester – an overview | ScienceDirect Topics

Mori, Satoka; Abe, Arisa; Ishikawa, Naoto; Rafique, Abdur; Ito, Yuji published an article in 2021, the title of the article was A novel site-specific chemical conjugation of IgG antibodies by affinity peptide for immunoassays.HPLC of Formula: 79642-50-5 And the article contains the following content:

Recently, there has been an increasing interest in site-specific modifications of antibodies used in immunoassays for disease diagnosis and as antibody therapeutics, such as antibody-drug conjugates. Previously, we established a site-specific chem. conjugation system using an IgG-Fc binding chem. conjugation affinity peptide (CCAP). CCAP could be used only for the modification of human IgG owing to the lack of affinity of CCAP to rodent IgG mols. In this study, novel CCAP reagents are proposed, which can be used for both human and mouse IgG, based on the Staphylococcus aureus protein A domain-derived affinity peptides Z34C and Z33. Compared with the activity of a conventional randomly modified antibody, mouse IgG modified using this method had favorable features in two immunoassays, demonstrating the advantages of the proposed CCAP method in preserving antibody functionality during conjugation. The experimental process involved the reaction of Bis(2,5-dioxopyrrolidin-1-yl) glutarate(cas: 79642-50-5).HPLC of Formula: 79642-50-5

The Article related to staphylococcus aureus igg monoclonal antibodies peptide immunoassay, rpla, antibody, conjugation, immunoassay, peptide, protein a, Placeholder for records without volume info and other aspects.HPLC of Formula: 79642-50-5

Referemce:
Ester – Wikipedia,
Ester – an overview | ScienceDirect Topics

On August 14, 2020, Feng, Shaojie; Xiong, Chenghe; Wang, Guirong; Wang, Subo; Jin, Guoxia; Gu, Guofeng published an article.Name: Bis(2,5-dioxopyrrolidin-1-yl) glutarate The title of the article was Exploration of Recombinant Fusion Proteins YAPO and YAPL as Carrier Proteins for Glycoconjugate Vaccine Design against Streptococcus pneumoniae Infection. And the article contained the following:

Pneumolysin (Ply), pneumococcal surface protein A (PspA), and pneumococcal surface adhesin A (PsaA) are promising cell surface protein antigen targets for Streptococcus pneumoniae (Spn) vaccine development. We designed and recombined 2 fusion proteins, named YAPO and YAPL, which contained the main antigenic epitopes of Ply, PspA, and PsaA. In-depth immunol. evaluations revealed that YAPO and YAPL had strong immunocompetence to be well-qualified potential carrier proteins. To verify this possibility, a serotype 3 Spn (ST3) capsular polysaccharide pentasaccharide was conjugated to each fusion protein to generate the resultant glycoconjugates. Immunol. studies in mice revealed that, as compared with TT conjugate, YAPO and YAPL conjugates provoked robust T-cell-dependent immune responses that could provide better recognition, in vitro efficient opsonophagocytosis, and in vivo effective protection against various serotypes of Spn. Collectively, YAPO and YAPL were identified as immunopotentiating carriers that could help convert immunol. inactive ST3 pentasaccharide into a T cell-dependent antigen and provide efficient and broad spectrum of immunoprotection coverage so as to formulate functional glycoconjugate vaccines against Spn infections. The experimental process involved the reaction of Bis(2,5-dioxopyrrolidin-1-yl) glutarate(cas: 79642-50-5).Name: Bis(2,5-dioxopyrrolidin-1-yl) glutarate

The Article related to streptococcus glycoconjugate vaccine yapo yapl carrier protein, streptococcus pneumoniae, carrier protein, fusion protein, glycoconjugate vaccine, immunoprotection, Placeholder for records without volume info and other aspects.Name: Bis(2,5-dioxopyrrolidin-1-yl) glutarate

Referemce:
Ester – Wikipedia,
Ester – an overview | ScienceDirect Topics

On June 30, 2020, Guo, Jiatong; Jiang, Wenjie; Li, Qingjiang; Jaiswal, Mohit; Guo, Zhongwu published an article.Product Details of 79642-50-5 The title of the article was Comparative immunological studies of tumor-associated Lewis X, Lewis Y, and KH-1 antigens. And the article contained the following:

Tumor-associated carbohydrate antigens Lewis X (Lex), Lewis Y (Ley), and KH-1 are useful targets for cancer immunotherapy. In this regard, an insight into the structure-immunogenicity relationships of these antigens is important but this has not been systematically investigated yet. In the current study, Lex, Ley, and KH-1 antigens with a lactose unit at the reducing end as a spacer were synthesized and coupled with keyhole limpet hemocyanin (KLH) protein. Immunol. evaluations of the resultant conjugates revealed that they all could elicit robust immune responses while the Ley conjugate could provoke the highest titers of total and IgG antibodies. The binding assays of their antisera to each antigen and to cancer cells showed that each antiserum had extensive cross-reaction with all three antigens as protein conjugates and strong but somewhat antigen-selective binding towards MCF-7 cancer cell. Moreover, none of these antisera had obvious binding to SKMEL-28 cancer cell that does not express Lex, Ley and KH-1. The results of assays of these antisera to mediate complement-dependent cytotoxicity (CDC) to MCF-7 and SKMEL-28 cancer cells were very similar to the results of binding assays. Thus, it was concluded that all three antigens could form effective conjugate vaccines whereas the Ley conjugate induced the most robust immune responses and the antiserum of Lex had the highest binding and cytotoxicity to target cancer cells. In addition, as the antibodies induced by each antigen had extensive cross-reaction with other two antigens, either Lex or Ley or the two combined can be utilized to formulate effective conjugate vaccines for cancer immunotherapy. Another paradigm-shifting discovery of this study is that the presentation of Lex, Ley, and KH-1 antigens on cancer cell can be different from that in synthetic conjugates, which should be taken into consideration during the design and optimization of related cancer vaccines or immunotherapies. The experimental process involved the reaction of Bis(2,5-dioxopyrrolidin-1-yl) glutarate(cas: 79642-50-5).Product Details of 79642-50-5

The Article related to carbohydrate lewisx lewisy kh1 antigen glycoconjugates cancer vaccine immunotherapy, cancer antigen, cancer vaccine, carbohydrate, glycoconjugate, kh-1, lewis x, lewis y, Placeholder for records without volume info and other aspects.Product Details of 79642-50-5

Referemce:
Ester – Wikipedia,
Ester – an overview | ScienceDirect Topics

On August 19, 2020, Lerchen, Hans-Georg; Stelte-Ludwig, Beatrix; Sommer, Anette; Berndt, Sandra; Rebstock, Anne-Sophie; Johannes, Sarah; Mahlert, Christoph; Greven, Simone; Dietz, Lisa; Joerissen, Hannah published an article.Category: esters-buliding-blocks The title of the article was Tailored Linker Chemistries for the Efficient and Selective Activation of ADCs with KSPi Payloads. And the article contained the following:

Several antibody-drug conjugates (ADCs) have failed to achieve a sufficiently large therapeutic window in patients due to toxicity induced by unspecific payload release in the circulation or ADC uptake into healthy organs. Herein, we describe the successful engineering of ADCs consisting of novel linkers, which are efficiently and selectively cleaved by the tumor-associated protease legumain. ADCs generated via this approach demonstrate high potency and a preferential activation in tumors compared to healthy tissue, thus providing an addnl. level of safety. A remarkable tolerance of legumain for different linker peptides, including those with just a single asparagine residue, together with a modifier of the physicochem. metabolite profile, proves the broad applicability of this approach for a tailored design of ADCs. The experimental process involved the reaction of Bis(2,5-dioxopyrrolidin-1-yl) glutarate(cas: 79642-50-5).Category: esters-buliding-blocks

The Article related to linker peptide antibody drug conjugate antitumor targeting tweakr, Pharmaceuticals: Formulation and Compounding and other aspects.Category: esters-buliding-blocks

Referemce:
Ester – Wikipedia,
Ester – an overview | ScienceDirect Topics

Lopez Rivas, Paula; Muller, Christoph; Breunig, Christian; Hechler, Torsten; Pahl, Andreas; Arosio, Daniela; Belvisi, Laura; Pignataro, Luca; Dal Corso, Alberto; Gennari, Cesare published an article in 2019, the title of the article was β-Glucuronidase triggers extracellular MMAE release from an integrin-targeted conjugate.Name: Bis(2,5-dioxopyrrolidin-1-yl) glutarate And the article contains the following content:

A non-internalizing αvβ3 integrin ligand was conjugated to the anticancer drug MMAE through a β-glucuronidase-responsive linker. In the presence of β-glucuronidase, only the conjugate bearing a PEG4 spacer inhibited the proliferation of integrin-expressing cancer cells at low nanomolar concentrations, indicating important structural requirements for the efficacy of these therapeutics. The experimental process involved the reaction of Bis(2,5-dioxopyrrolidin-1-yl) glutarate(cas: 79642-50-5).Name: Bis(2,5-dioxopyrrolidin-1-yl) glutarate

The Article related to glucuronidase extracellular mmae release integrin targeted conjugate, Pharmaceuticals: Formulation and Compounding and other aspects.Name: Bis(2,5-dioxopyrrolidin-1-yl) glutarate

Referemce:
Ester – Wikipedia,
Ester – an overview | ScienceDirect Topics

Mukerjee, Anindita; Ranjan, Amalendu P.; Vishwanatha, Jamboor K. published an article in 2014, the title of the article was Non-covalent surface integration: optimising a novel technique for preparing targeted polymeric nanoparticles for cancer therapeutics.SDS of cas: 79642-50-5 And the article contains the following content:

Targeting anticancer drugs to their specific mol. targets is a major challenge in cancer therapy. However, advances in biomedical and protein engineering have led to novel nanoparticle targeting approaches. In this study, we used a novel non-covalent insertion of a homo-bifunctional spacer for targeted delivery of drugs to various cancer cells. Functionalised blank nanoparticles for antibody (targeting agent) conjugation were prepared using different crosslinking spacers (bis[sulfosuccinimidyl] suberate (BS3), Disuccinimidyl glutarate (DSG) and sulfo-N-[ε-maleimidocaproyloxy] sulfosuccinimide ester (s-EMCS)). The concentration of the spacers and the concentration of antibody used for conjugation were optimized using flow cytometry. The optimized and functionalised nanoparticles thus obtained were characterised for percent yield, mean particle size, surface morphol. and percent antibody attachment. Our studies showed the formation of smooth and spherical functionalised poly(D,L-lactide-co-glycolide) (PLGA) nanoparticles which could be successfully conjugated to an antibody, Anti-Annexin A2, for targeting to breast cancer cells. The functionalisation of PLGA nanoparticles for antibody attachment was effectively optimized leading to high percent attachments of 92.8% achieved with BS3. Antibody conjugated PLGA nanoparticles were then evaluated for their targeting potential. Robust intra-cellular uptake of the targeted nanoparticles was observed in breast cancer cell line and in mouse xenograft tumor studies. Our results thus validate that such a novel technique of surface integration may be used for preparing targeted polymeric nanoparticles for cancer therapeutics. The experimental process involved the reaction of Bis(2,5-dioxopyrrolidin-1-yl) glutarate(cas: 79642-50-5).SDS of cas: 79642-50-5

The Article related to non covalent surface integration polymeric nanoparticle cancer therapeutics, Pharmaceuticals: Formulation and Compounding and other aspects.SDS of cas: 79642-50-5

Referemce:
Ester – Wikipedia,
Ester – an overview | ScienceDirect Topics

On July 31, 2021, Zhang, Yu; Liu, Jia; Yu, Dandan; Zhu, Xinxin; Liu, Xiaoyan; Liao, Jun; Li, Sheng; Wang, Huayi published an article.SDS of cas: 79642-50-5 The title of the article was The MLKL kinase-like domain dimerization is an indispensable step of mammalian MLKL activation in necroptosis signaling. And the article contained the following:

MLKL phosphorylation by RIP3 is the commitment step of necroptosis execution, which could induce MLKL activation featured as MLKL monomer-oligomer transition. Here, we reported that the dimerization of the MLKL kinase-like domain was the direct consequence of RIP3 triggered MLKL-phosphorylation. Two inter-dimer interfaces were found in the crystal structure of human MLKL. Mutations destroying both interfaces could prevent RIP3-induced MLKL oligomerization and necroptosis efficiently. Moreover, we confirmed MLKL self-assembly by the internal coiled-coil region is necessary for MLKL oligomerization and function. The mutations disrupting coiled-coil self-assembly repressed necroptosis, but it did not prevent RIP3-induced dimerization of the MLKL kinase-like domain. So that, MLKL activation is a sequential process, which begins with kinase-like domain dimerization, and followed by internal coiled-coil region self-assembly to form a proper MLKL oligomer. Besides human MLKL, structural and functional anal. showed the kinase-like domain dimerization was conserved among mammalian species, suggesting it is a general step of the RIP3-induced MLKL activation process. The experimental process involved the reaction of Bis(2,5-dioxopyrrolidin-1-yl) glutarate(cas: 79642-50-5).SDS of cas: 79642-50-5

The Article related to mlkl domain dimerization necroptosis signaling, Mammalian Biochemistry: Development and Aging and other aspects.SDS of cas: 79642-50-5

Referemce:
Ester – Wikipedia,
Ester – an overview | ScienceDirect Topics

van Dongen, Stijn F. M.; Maiuri, Paolo; Marie, Emmanuelle; Tribet, Christophe; Piel, Matthieu published an article in 2013, the title of the article was Triggering Cell Adhesion, Migration or Shape Change with a Dynamic Surface Coating.Category: esters-buliding-blocks And the article contains the following content:

The authors here report a strategy for study of cell dynamics that involves only azido-(PLL-g-PEG) (APP) and the addition of a reactive BCN-RGD peptide to the cell culture medium as a trigger. APP and BCN-RGD allow the noninvasive ‘switching on’ of cell adhesion with very high contrast, because the adhesion mol. is only introduced when desired, leaving the ‘switched off’ surface featureless. To demonstrate the versatility of this approach, the authors show a set of experiments that validate the trigger. Then, the authors combine it with patterned surfaces. Patterns allow for interesting applications where cell adhesion is triggered while cells are already attached to certain areas of the substrate (in situ triggering). As typical applications, the authors show the induction of both single and collective cell migration, create cocultures, and trigger the synchronous control of cell shape change, illustrating dynamic control. The experimental process involved the reaction of Bis(2,5-dioxopyrrolidin-1-yl) glutarate(cas: 79642-50-5).Category: esters-buliding-blocks

The Article related to cell adhesion migration shape dynamic surface coating, Biochemical Methods: Culture and Preservation and other aspects.Category: esters-buliding-blocks

Referemce:
Ester – Wikipedia,
Ester – an overview | ScienceDirect Topics

Menegatti, Stefano; Hussain, Mahmud; Naik, Amith D.; Carbonell, Ruben G.; Rao, Balaji M. published an article in 2013, the title of the article was mRNA display selection and solid-phase synthesis of Fc-binding cyclic peptide affinity ligands.Computed Properties of 79642-50-5 And the article contains the following content:

Cyclic peptides are attractive candidates for synthetic affinity ligands due to their favorable properties, such as resistance to proteolysis, and higher affinity and specificity relative to linear peptides. Here we describe the discovery, synthesis and characterization of novel cyclic peptide affinity ligands that bind the Fc portion of human IgG (IgG; hFc). We generated an mRNA display library of cyclic pentapeptides wherein peptide cyclization was achieved with high yield and selectivity, using a solid-phase crosslinking reaction between two primary amine groups, mediated by a homobifunctional linker. Subsequently, a pool of cyclic peptide binders to hFc was isolated from this library and chromatog. resins incorporating the selected cyclic peptides were prepared by on-resin solid-phase peptide synthesis and cyclization. Significantly, this approach results in resins that are resistant to harsh basic conditions of column cleaning and regeneration. Further studies identified a specific cyclic peptide-cyclo[Link-M-WFRHY-K]-as a robust affinity ligand for purification of IgG from complex mixtures The cyclo[Link-M-WFRHY-K] resin bound selectively to the Fc fragment of IgG, with no binding to the Fab fragment, and also bound Igs from a variety of mammalian species. Notably, while the recovery of IgG using the cyclo[Link-M-WFRHY-K] resin was comparable to a Protein A resin, elution of IgG could be achieved under milder conditions (pH 4 vs. pH 2.5). Thus, cyclo[Link-M-WFRHY-K] is an attractive candidate for developing a cost-effective and robust chromatog. resin to purify monoclonal antibodies (mAbs). Finally, our approach can be extended to efficiently generate and evaluate cyclic peptide affinity ligands for other targets of interest. The experimental process involved the reaction of Bis(2,5-dioxopyrrolidin-1-yl) glutarate(cas: 79642-50-5).Computed Properties of 79642-50-5

The Article related to mrna display library cyclic peptide fc binding antibody purification, Immunochemistry: Methods (Including Analysis) and other aspects.Computed Properties of 79642-50-5

Referemce:
Ester – Wikipedia,
Ester – an overview | ScienceDirect Topics