134978-99-7Relevant articles and documents
Spacer molecules in peptide sequences: Incorporation into analogues of atrial natriuretic factor
Boumrah, Deradji,Campbell, Malcolm M.,Fenner, Simon,Kinsman, Richard G.
, p. 7735 - 7738 (1991)
The spacer reagents FmocHN(CH2CH2CH2)3CH 2COOPfp (1b) and FmocHN(CH2CH2O) 3CH2COOPfp (2d) have been prepared and used to substitute for tetra-residue sequences in the cyclic portion of Atrial Natriuretic Factor (ANF) by solid phase peptide assembly.
Spacer molecules in peptide sequences: Incorporation into analogues of atrial natriuretic factor
Boumrah, Derradji,Campbell, Malcolm M.,Fenner, Simon,Kinsman, Richard G.
, p. 6977 - 6992 (1997)
In the present study, 10 modified human atrial natriuretic factor (hANF) analogues were designed using solid phase synthesis. This was carried out by replacing 'alkyl or glycol' spacer with octapeptide sequence within die cyclic portion of hANF in each annlogue synthesised. The unnatural amino acid spacers (1b) and (2d) have been synthesised using solution chemistry. The latter spacers were successfully incorporated into the peptide structure, using solid phase synthesis assembly. Amongst the ten analogues, thus prepared, two in which the alkyl spacer was used to substitute amino acid residues Gly15 to Gly21 and Arg14 to Leu21 to give 4a and 4b, successively. In the purification process of the latter analogues (4a, 4b), problems of their severe solubility were encountered. The eight glycol-spaced analogues (5a-5h) were successfully synthesised and purified using HPLC. The structure of (5a-5h) was confirmed by the presence of mass ion peaks in the atom bombardment mass spectroscopy (FAB MS) and by NMR. The latter analogues were tested, in vivo, for their ability to bind to specific hANF receptors, as agonists or antagonists. The biological results have showed that none of these analogues (5a-5h) were active.
Synthesis of a polymerizable metal-ion-chelating lipid for fluid bilayers
Sang Won Jeong,O'Brien
, p. 4799 - 4802 (2001)
Hydrated lipid structures, such as liposomes, that display tethered metal-ion-chelating groups have proven useful in peptide and protein binding, as well as 2D protein crystallization through molecular recognition of accessible histidine sites in proteins and peptides. Polymerizable metal-ion-chelating lipids bearing a reactive diacetylene group have been described. These interesting compounds can be polymerized in the solid-analogous phase. Here we describe the design of the first polymerizable metal-ion-chelating lipid that can be used in the fluid, i.e., liquid analogous, phase of lipid bilayers. The synthesis of 1-palmitoyl-2-[8-[(E,E)-2′,4′-hexadienoyloxy] octanoyl]-sn-glycero-3-N-[11-[N′,N′bis- [carboxymethyl]imino]-3,6,9-trioxaundecanoyl] phosphatidylethanolamine (1) is described. The chelator moiety, iminodiacetate (IDA), was linked to the polymerizable phosphatidylethanolamine (PE) with a terminal 2,4-hexadienoyl (sorbyl) group through an oligo(ethylene glycol)-based spacer. Lipid 1-Cu complex is designed to be combined with the corresponding polymerizable matrix lipids (bis-SorbPC) to form functionalized liposomes that can be stabilized by various polymerization methods.
Optimization of IEDDA bioorthogonal system: Efficient process to improve trans-cyclooctene/tetrazine interaction
Béquignat, Jean-Baptiste,Boucheix, Claude,Canitrot, Damien,Chezal, Jean-Michel,Degoul, Fran?oise,Miot-Noirault, Elisabeth,Moreau, Emmanuel,Navarro-Teulon, Isabelle,Quintana, Mercedes,Rondon, Aurélie,Taiariol, Ludivine,Ty, Nancy
supporting information, (2020/07/21)
The antibody pretargeting approach for radioimmunotherapy (RIT) using inverse electron demand Diels-Alder cycloaddition (IEDDA) constitutes an emerging theranostic approach for solid cancers. However, IEDDA pretargeting has not reached clinical trial. The major limitation of the IEDDA strategy depends largely on trans-cyclooctene (TCO) stability. Indeed, TCO may isomerize into the more stable but unreactive cis-cyclooctene (CCO), leading to a drastic decrease of IEDDA efficiency. We have thus developed both efficient and reproducible synthetic pathways and analytical follow up for (PEGylated) TCO derivatives, providing high TCO isomeric purity for antibody modification. We have set up an original process to limit the isomerization of TCO to CCO before the mAbs’ functionalization to allow high TCO/tetrazine cycloaddition.
Small molecule microarray-facilitated screening of affinity-based probes (AfBPs) for γ-secretase
Shi, Haibin,Liu, Kai,Xu, Ashley,Yao, Shao Q.
supporting information; experimental part, p. 5030 - 5032 (2010/01/06)
A small molecule microarray (SMM) platform is developed herein, which enables high-throughput discovery of affinity-based probes (AfBPs) against γ-secretase.
Functional determinants of a synthetic vesicle fusion system
Gong, Yun,Ma, Mingming,Luo, Yumei,Bong, Dennis
, p. 6196 - 6205 (2008/12/20)
Selective membrane mergers may be driven by small-molecule recognition between synthetic surface-displayed fusogens which bear vancomycin glycopeptide and its native binding target, D-Ala-D-Ala dipeptide. These recognition motifs are membrane anchored by
Membrane activation: Selective vesicle fusion via small molecule recognition
Gong, Yun,Luo, Yumei,Bong, Dennis
, p. 14430 - 14431 (2008/01/27)
We report herein the induction of selective vesicle fusion with biological recognition motifs not natively associated with lipid bilayer fusion, thus broadening the scope of recognition-guided membrane activation. Our system employs vancomycin glycopeptid
Highly sensitive detection of GG mismatched DNA by surfaces immobilized naphthyridine dimer through poly(ethylene oxide) linkers
Nakatani, Kazuhiko,Kobori, Akio,Kumasawa, Hiroyuki,Saito, Isao
, p. 1105 - 1108 (2007/10/03)
Naphthyridine dimer is a unique molecule that strongly, and selectively, binds to the guanine-guanine mismatch in duplex DNA. We have synthesized naphthyridine dimers possessing a different length of poly(ethylene oxide) (PEO) linker, and immobilized them
