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132178-37-1

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132178-37-1 Usage

General Description

2,5-Pyrrolidinedione, 1-[(1-oxo-4-pentynyl)oxy]- is a chemical compound with the molecular formula C10H11NO3. It is a heterocyclic compound containing a pyrrolidinedione ring and an alkyne group. 2,5-Pyrrolidinedione, 1-[(1-oxo-4-pentynyl)oxy]- is used in organic synthesis and pharmaceutical research as a building block for the synthesis of various organic compounds and drugs. It has potential applications in the development of pharmaceuticals, as well as in the production of specialty chemicals and materials. Its properties and structure make it a valuable addition to the field of chemical research and development.

Check Digit Verification of cas no

The CAS Registry Mumber 132178-37-1 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,3,2,1,7 and 8 respectively; the second part has 2 digits, 3 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 132178-37:
(8*1)+(7*3)+(6*2)+(5*1)+(4*7)+(3*8)+(2*3)+(1*7)=111
111 % 10 = 1
So 132178-37-1 is a valid CAS Registry Number.

132178-37-1Relevant articles and documents

The Synthesis of a Multiblock Osteotropic Polyrotaxane by Copper(I)-Catalyzed Huisgen 1,3-Dipolar Cycloaddition

Hein, Christopher D.,Liu, Xin-Ming,Chen, Fu,Cullen, Diane M.,Wang, Dong

, p. 1544 - 1556 (2010)

The design and synthesis of a novel bone-targeting polyrotaxane delivery system that utilizes alendronate (ALN) as targeting moiety is presented in this manuscript. For the introduction of ALN, it is first conjugated to α-cyclodextrin (α-CD) and subsequen

Design of Polysaccharide-b-Elastin-Like Polypeptide Bioconjugates and Their Thermoresponsive Self-Assembly

Xiao, Ye,Chinoy, Zoeisha S.,Pecastaings, Gilles,Bathany, Katell,Garanger, Elisabeth,Lecommandoux, Sébastien

, p. 114 - 125 (2020)

The advantageous biological properties of polysaccharides and precise stimuli-responsiveness of elastin-like polypeptides (ELPs) are of great interest for the design of polysaccharide- A nd polypeptide-based amphiphilic block copolymers for biomedical applications. Herein, we report the synthesis and characterization of a series of polysaccharide-block-ELP copolymers, containing two biocompatible and biodegradable blocks coupled via copper(I)-catalyzed azide-alkyne cycloaddition (CuAAC). The resulting bioconjugates are capable of self-assembling into well-defined nanoparticles in aqueous solution upon raising the solution temperature above a specific transition temperature (Tt)- A characteristic of the ELP moiety. To the best of our knowledge, this is the first study where polysaccharides were combined with a stimuli-responsive ELP for the preparation of thermosensitive self-assemblies, providing insight into novel pathways for designing bioinspired stimuli-responsive self-assemblies for biomedical applications.

Synthesis and biochemical evaluation of cephalosporin analogues equipped with chemical tethers

Duhme-Klair, Anne-Kathrin,Gyulev, Ivan,Herman, Reyme,Krauss, Thomas F.,Miller, Lisa M.,Thomas, Gavin H.

, p. 36485 - 36494 (2020)

Molecular probes typically require structural modifications to allow for the immobilisation or bioconjugation with a desired substrate but the effects of these changes are often not evaluated. Here, we set out to determine the effects of attaching functio

Convenient synthesis of heterobifunctional poly(ethylene glycol) suitable for the functionalization of iron oxide nanoparticles for biomedical applications

Passemard, Solene,Staedler, Davide,Ucnova, Lucia,Schneiter, Guillaume Stephane,Kong, Phally,Bonacina, Luigi,Juillerat-Jeanneret, Lucienne,Gerber-Lemaire, Sandrine

, p. 5006 - 5010 (2013)

A straightforward route is proposed for the multi-gram scale synthesis of heterobifunctional poly(ethylene glycol) (PEG) oligomers containing combination of triethyloxysilane extremity for surface modification of metal oxides and amino or azido active end groups for further functionalization. The suitability of these PEG derivatives to be conjugated to nanomaterials was shown by pegylation of ultrasmall superparamagnetic iron oxide (USPIO) nanoparticles (NPs), followed by functionalization with small peptide ligands for biomedical applications.

Synthesis and biological evaluation of RGD and isoDGR peptidomimetic-α-amanitin conjugates for tumor-targeting

Bodero, Lizeth,Rivas, Paula López,Korsak, Barbara,Hechler, Torsten,Pahl, Andreas,Müller, Christoph,Arosio, Daniela,Pignataro, Luca,Gennari, Cesare,Piarulli, Umberto

, p. 407 - 415 (2018)

RGD-α-amanitin and isoDGR-α-amanitin conjugates were synthesized by joining integrin ligands to α-amanitin via various linkers and spacers. The conjugates were evaluated for their ability to inhibit biotinylated vitronectin binding to the purified αVβ3 receptor, retaining good binding affinity, in the same nanomolar range as the free ligands. The antiproliferative activity of the conjugates was evaluated in three cell lines possessing different levels of αVβ3 integrin expression: human glioblastoma U87 (αVβ3+), human lung carcinoma A549 (αVβ3?) and breast adenocarcinoma MDA-MB-468 (αVβ3?). In the U87, in the MDA-MB-468, and partly in the A549 cancer cell lines, the cyclo[DKP-isoDGR]-α-amanitin conjugates bearing the lysosomally cleavable Val-Ala linker were found to be slightly more potent than α-amanitin. Apparently, for all these α-amanitin conjugates there is no correlation between the cytotoxicity and the expression of αVβ3 integrin. To determine whether the increased cytotoxicity of the cyclo[DKP-isoDGR]-α-amanitin conjugates is governed by an integrin-mediated binding and internalization process, competition experiments were carried out in which the conjugates were tested with U87 (αVβ3+, αVβ5+, αVβ6?, α5β1+) and MDA-MB-468 (αVβ3?, αVβ5+, αVβ6+, α5β1?) cells in the presence of excess cilengitide, with the aim of blocking integrins on the cell surface. Using the MDA-MB-468 cell line, a fivefold increase of the IC50 was observed for the conjugates in the presence of excess cilengitide, which is known to strongly bind not only αVβ3, but also αVβ5, αVβ6, and α5β1. These data indicate that in this case the cyclo[DKP-isoDGR]-α-amanitin conjugates are possibly internalized by a process mediated by integrins different from αVβ3 (e.g., αVβ5).

Nanopharmacological Force Sensing to Reveal Allosteric Coupling in Transporter Binding Sites

Zhu, Rong,Sinwel, Doris,Hasenhuetl, Peter S.,Saha, Kusumika,Kumar, Vivek,Zhang, Peng,Rankl, Christian,Holy, Marion,Sucic, Sonja,Kudlacek, Oliver,Karner, Andreas,Sandtner, Walter,Stockner, Thomas,Gruber, Hermann J.,Freissmuth, Michael,Hauck Newman, Amy,Sitte, Harald H.,Hinterdorfer, Peter

, p. 1719 - 1722 (2016)

Controversy regarding the number and function of ligand binding sites in neurotransmitter/sodium symporters arose from conflicting data in crystal structures and molecular pharmacology. Here, we have designed novel tools for atomic force microscopy that directly measure the interaction forces between the serotonin transporter (SERT) and the S- and R-enantiomers of citalopram on the single molecule level. This approach is based on force spectroscopy, which allows for the extraction of dynamic information under physiological conditions thus inaccessible via X-ray crystallography. Two distinct populations of characteristic binding strengths of citalopram to SERT were revealed in Na+-containing buffer. In contrast, in Li+-containing buffer, SERT showed only low force interactions. Conversely, the vestibular mutant SERT-G402H merely displayed the high force population. These observations provide physical evidence for the existence of two binding sites in SERT when accessed in a physiological context. Competition experiments revealed that these two sites are allosterically coupled and exert reciprocal modulation.

"Click chemistry" in the preparation of porous polymer-based particulate stationary phases for μ-HPLC separation of peptides and proteins

Slater, Michael,Snauko, Marian,Svec, Frantisek,Frechet, Jean M. J.

, p. 4969 - 4975 (2006)

With the use of the copper(I)-catalyzed (3 + 2) azide-alkyne cycloaddition, an element of "click chemistry," stationary phases carrying long alkyl chains or soybean trypsin inhibitor have been prepared for use in HPLC separations in the reversed-phase and affinity modes, respectively. The ligands were attached via a triazole ring to size monodisperse porous beads containing either alkyne or azide pendant functionalities. Alkyne-containing beads prepared by direct copolymerization of propargyl acrylate with ethylene dimethacrylate were allowed to react with azidooctadecane to give a reversed-phase sorbent. Azide-functionalized beads were prepared by chemical modification of glycidyl methacrylate particles. Subsequent reaction with a terminal aliphatic alkyne produced a reversed-phase sorbent similar to that obtained from the alkyne beads. Soybean trypsin inhibitor was functionalized with N-(4-pentynoyloxy) succinimide to carry alkyne groups and then allowed to react with the azide-containing beads to produce an affinity sorbent for trypsin. The performance of these stationary phases was demonstrated with the HPLC separations of a variety of peptides and proteins.

Constructing hybrid protein zymogens through protective dendritic assembly

Ng, David Y. W.,Arzt, Matthias,Wu, Yuzhou,Kuan, Seah Ling,Lamla, Markus,Weil, Tanja

, p. 324 - 328 (2014)

The modulation of protein uptake and activity in response to physiological changes forms an integral part of smart protein therapeutics. We describe herein the self-assembly of a pH-responsive dendrimer shell onto the surface of active enzymes (trypsin, papain, DNase I) as a supramolecular protecting group to form a hybrid dendrimer-enzyme complex. The attachment is based on the interaction between boronic acid and salicyl hydroxamate, thus allowing the macromolecular assembly to respond to changes in pH between 5.0 and 7.4 in a highly reversible fashion. Catalytic activity is efficiently blocked in the presence of the dendrimer shell but is quantitatively restored upon shell degradation under acidic conditions. Unlike the native proteases, the hybrid constructs are shown to be efficiently taken up by A549 cells and colocalized in the acidic compartments. The programmed intracellular release of the proteases induced cytotoxicity, thereby uncovering a new avenue for precision biotherapeutics. The programmed self-assembly of a dendritic shell onto enzymes was used to modulate enzyme activity as well as induce cellular entry and release of the active proteins. The defined dendritic construct represents a contemporary avenue for smart protein therapeutics. Copyright

MODIFIED MULTIMERIC BICYCLIC PEPTIDE LIGANDS

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Page/Page column 34; 35, (2021/02/19)

The present invention relates to multimers of polypeptides which are covalently bound to molecular scaffolds such that two or more peptide loops are subtended between attachment points to the scaffold, characterised in that said multimeric binding complex additionally comprises a modifier group conjugated thereto. The invention also describes the multimerization of polypeptides through various chemical linkers and hinges of various lengths and rigidity using different sites of attachments within polypeptides. In particular, the invention describes multimers of peptides which are high affinity binders and activators of CD137. The invention also includes drug conjugates comprising said multimeric binding complexes, conjugated to one or more effector and/or functional groups, to pharmaceutical compositions comprising said multimeric binding complexes and drug conjugates and to the use of said multimeric binding complexes and drug conjugates in preventing, suppressing or treating a disease or disorder mediated by CD137 and to the use in an analytical method (i.e. as a tracer or a tag).

ANTIBODY FUNCTIONALISATION

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Page/Page column 35, (2020/12/07)

The present invention relates to a method of acylating lysine residues on antibodies using a thioester as the acylating reagent, wherein the thioester first reacts with a cysteine residue of the antibody, before the acyl moiety is transferred to a proxima

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