93892-06-9Relevant articles and documents
SITE-SPECIFIC RADIOFLUORINATION OF PEPTIDES WITH 8-[18F]-FLUOROOCTANOIC ACID CATALYZED BY LIPOIC ACID LIGASE
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Paragraph 00207, (2017/12/28)
New methodologies for site-specifically radiolabeling proteins with the PET isotope [18F] are required to generate high quality radiotracers for imaging in both the preclinical and clinical settings. The enzymatic radiofluorination overcomes many of the limitations encountered to date with purely chemical approaches. The bacterial enzyme lipoic acid ligase was used to conjugate [18F]-fluorooctanoic acid to both a small peptide and a Fab antibody fragment. Labeling was site-specific and highly efficient under mild aqueous conditions using small amounts of peptide/protein (1-10 nmol). The labeled construct retained full epitope binding affinity and was stable in mouse serum. Using an optimized reaction scheme, mCi quantities of [18F]-Fab were generated, an amount sufficient for human imaging.
NOVEL DIHYDROXYBENZENE DERIVATIVES AND ANTIPROTOZOAL AGENT COMPRISING SAME AS ACTIVE INGREDIENT
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Paragraph 0102; 0104; 0105, (2013/09/26)
Novel compounds below are useful for preventing or treating diseases caused by protozoans. At least one of a compound represented by Formula (I) (wherein, X represents a hydrogen atom or a halogen atom; R1 represents a hydrogen atom; R2 represents a hydrogen atom or a C1-7 alkyl group; R3 represents -CHO, -C(=O)R5, -COOR5 (wherein R5 represents a C1-7 alkyl group), -CH2OH or -COOH; and R4 represents a C1-16 alkyl group having one or more substituents on a terminal carbon atom and/or non-terminal carbon atom(s), a C2-16 alkenyl group having one or more substituents on a terminal carbon atom and/or non-terminal carbon atom(s), or a C2-16 alkynyl group having one or more substituents on a terminal carbon atom and/or non-terminal carbon atom(s)), an optical isomer thereof, and a pharmaceutically acceptable salt is used.
Potent oligomerization and macrocyclization activity of the thioesterase domain of vicenistatin polyketide synthase
Kudo, Fumitaka,Asou, Yusaku,Watanabe, Moe,Kitayama, Takashi,Eguchi, Tadashi
supporting information; experimental part, p. 1843 - 1846 (2012/08/29)
The thioesterase domain of the polyketide synthase involved in the biosynthesis of the 20-membered macrolactam antibiotic vicenistatin (VinTE) was found to catalyze oligomerization and macrocyclization of ω-hydroxy fatty acid ethyl esters to afford 17-28-membered macrocyclic lactones. The ring sizes of the macrocycles appear to be limited to the more moderate sizes because of the space limitation of the active site of VinTE. It was also verified that the initially formed linear dimer is first released from the active site of VinTE and then is recognized again by VinTE prior to its transformation to the cyclic dimer.
