51795-97-2Relevant articles and documents
Copper-Catalyzed Alkoxycarbonylation of Alkyl Iodides for the Synthesis of Aliphatic Esters: Hydrogen Makes the Difference
Geng, Hui-Qing,Wu, Xiao-Feng
supporting information, p. 8062 - 8066 (2021/10/25)
A copper-catalyzed alkoxycarbonylation transformation of unactivated alkyl iodides has been developed. Various alkyl iodides can be converted into the corresponding tert-butyl esters in good yields. NaOtBu acts as both a nucleophile and a base. Moreover, other types of aliphatic esters can also be obtained in moderated yields if extra alcohols are added. Both primary and secondary alkyl alcohols can react successfully.
Chemoselective and Site-Selective Lysine-Directed Lysine Modification Enables Single-Site Labeling of Native Proteins
Adusumalli, Srinivasa Rao,Kalra, Neetu,Purushottam, Landa,Rai, Vishal,Rawale, Dattatraya Gautam,Reddy, Neelesh C.,Shukla, Sanjeev,Thakur, Kalyani
supporting information, p. 10332 - 10336 (2020/04/27)
The necessity for precision labeling of proteins emerged during the efforts to understand and regulate their structure and function. It demands selective attachment of tags such as affinity probes, fluorophores, and potent cytotoxins. Here, we report a method that enables single-site labeling of a high-frequency Lys residue in the native proteins. At first, the enabling reagent forms stabilized imines with multiple solvent-accessible Lys residues chemoselectively. These linchpins create the opportunity to regulate the position of a second Lys-selective electrophile connected by a spacer. Consequently, it enables the irreversible single-site labeling of a Lys residue independent of its place in the reactivity order. The user-friendly protocol involves a series of steps to deconvolute and address chemoselectivity, site-selectivity, and modularity. Also, it delivers ordered immobilization and analytically pure probe-tagged proteins. Besides, the methodology provides access to antibody-drug conjugate (ADC), which exhibits highly selective anti-proliferative activity towards HER-2 expressing SKBR-3 breast cancer cells.
CHEMOSELECTIVE SENSITIVITY BOOSTER FOR TAGGING A PEPTIDE, PEPTIDE CONJUGATE, OR SIMILAR REACTIVE MOLECULE
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Page/Page column 41, (2020/12/29)
The invention pertains to chemoselective sensitivity booster for tagging a peptide, peptide conjugate, or similar reactive molecule for analysis of a peptide, protein, antibody, protein bioconjugate, antibody bioconjugate, and similar analytes. The sensitivity booster comprises of sp2 or sp3 nitrogen centers in combination with hydrophobic carbon chains linked with an electrophile or nucleophile for attachment with a peptide, peptide conjugate, or molecules with similar reactivity.
Sensitivity booster for mass detection enables unambiguous analysis of peptides, proteins, antibodies, and protein bioconjugates
Singudas, Rohith,Reddy, Neelesh C.,Rai, Vishal
, p. 9979 - 9982 (2019/08/22)
A chemical tag enhances peptide detection by multiple orders in mass spectrometry. The substantial improvement in the peptide mapping along with simplified and enhanced fragmentation pattern enables the unambiguous sequencing of a protein and antibody. The chemoselective sensitivity booster provides a tool for remarkably improved analysis of protein bioconjugates.
Encapsulating propeller-like columnar liquid crystals with an aromatic outer shell: Influence of phenoxy-terminated side chains on the phase behaviour of triphenylbenzenes
Bader, Korinna,W?hrle, Tobias,?ztürk, Esra,Baro, Angelika,Laschat, Sabine
, p. 6409 - 6414 (2018/08/17)
Tailoring of phase transition temperatures of columnar liquid crystals by side chain variation is often associated with an undesired change in the mesophase type and/or geometry. To overcome this problem phenoxy-terminated side chains rather than alkyl si
Single-Site Labeling of Native Proteins Enabled by a Chemoselective and Site-Selective Chemical Technology
Adusumalli, Srinivasa Rao,Rawale, Dattatraya Gautam,Singh, Usha,Tripathi, Prabhanshu,Paul, Rajesh,Kalra, Neetu,Mishra, Ram Kumar,Shukla, Sanjeev,Rai, Vishal
supporting information, p. 15114 - 15123 (2018/11/10)
Chemical biology research often requires precise covalent attachment of labels to the native proteins. Such methods are sought after to probe, design, and regulate the properties of proteins. At present, this demand is largely unmet due to the lack of empowering chemical technology. Here, we report a chemical platform that enables site-selective labeling of native proteins. Initially, a reversible intermolecular reaction places the "chemical linchpins" globally on all the accessible Lys residues. These linchpins have the capability to drive site-selective covalent labeling of proteins. The linchpin detaches within physiological conditions and capacitates the late-stage installation of various tags. The chemical platform is modular, and the reagent design regulates the site of modification. The linchpin is a multitasking group and facilitates purification of the labeled protein eliminating the requirement of additional chromatography tag. The methodology allows the labeling of a single protein in a mixture of proteins. The precise modification of an accessible residue in protein ensures that their structure remains unaltered. The enzymatic activity of myoglobin, cytochrome C, aldolase, and lysozyme C remains conserved after labeling. Also, the cellular uptake of modified insulin and its downstream signaling process remain unperturbed. The linchpin directed modification (LDM) provides a convenient route for the conjugation of a fluorophore and drug to a Fab and monoclonal antibody. It delivers trastuzumab-doxorubicin and trastuzumab-emtansine conjugates with selective antiproliferative activity toward Her-2 positive SKBR-3 breast cancer cells.
Aldehydes can switch the chemoselectivity of electrophiles in protein labeling
Adusumalli, Srinivasa Rao,Rawale, Dattatraya Gautam,Rai, Vishal
supporting information, p. 9377 - 9381 (2019/01/03)
We show that the chemoselectivity of an electrophile in protein labeling can be promiscuous. An aldehyde enables switching of chemoselectivity of an epoxide and a sulfonate ester along with an enhanced rate of reaction. The chemical technology renders single-site installation of diverse probes on a protein and delivers analytically pure tagged proteins.
2-AMINO-1,3,4-THIADIAZINE AND 2-AMINO-1,3,4-OXADIAZINE BASED ANTIFUNGAL AGENTS
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Page/Page column 77; 78, (2017/02/09)
The invention provides a compound which is a diazine of formula (I) or a tautomer thereof, or a pharmaceutically acceptable salt thereof, for use as an antifungal agent: (I) wherein X, N', C', A and E are as defined herein. The invention also provides a compound of Formula (I) as defined herein.
Zirconium complexes with pendant aryloxy groups attached to the metallocene moiety by ethyl or hexyl spacers
Cho, Won Seok,Kim, So Han,Kim, Da Jung,Mun, Sang-Deok,Kim, Ran,Go, Min Jeong,Park, Myung Hwan,Kim, Min,Lee, Junseong,Kim, Youngjo
, p. 205 - 212 (2013/10/22)
Four zirconium complexes with pendant aryloxy groups attached to the metallocene moiety by ethyl or hexyl spacers have been synthesized and characterized by spectroscopic methods and HR-MS or elemental analysis. The solid state structure of bis[{6-(2,6-dimethylphenoxy)hexyl}cyclopentadienyl] zirconium dichloride was determined by single crystal X-ray diffraction. The prepared complexes were tested as catalyst precursors in the polymerization of ethylene upon activation with MAO. The results showed a marked effect of the spacer length on the catalytic activity, while only a minor effect of the substitution on the aryl group, which affected its steric properties.
1-Phenoxyalkyl-4-[(N,N-disubstitutedamino)alkyl]piperazine derivatives as non-imidazole histamine H3-antagonists
Staszewski, Marek,Walczynski, Krzysztof
, p. 1287 - 1304 (2013/04/10)
In this study, a series of 1-phenoxyalkyl-4-[(N,N-disubstitutedamino)alkyl] piperazine derivatives has been prepared and in vitro tested as H 3-receptor antagonists (electrically evoked contraction of the guinea pig jejunum). All compounds inve