328273-17-2

Usage

Uses

Used in Pharmaceutical Industry:
(3aS,4S,6aR)-N-[5-[(1,1-dimethylethoxy)carbonyl]aminopentyl]hexahydro-2-oxo-1H-thieno[3,4-d]imidazole-4-pentanamide is used as a potential pharmaceutical candidate for various applications due to its complex molecular structure and the presence of multiple functional groups. Its potential interactions with biological targets, such as enzymes or receptors, make it a promising compound for further research and development in the pharmaceutical industry. However, additional studies are required to determine its specific biological activities and potential therapeutic uses.

Upstream product

• 51644-96-3 5-tert-butoxycarbonylamino-1-aminopentane 
• 58-85-5 biotin 

Downstream Products

• 288259-39-2 5-((+)-biotinamido)pentylamine trifluoroacetic acid 
• 1031858-01-1 C₄₈H₄₉BF₂N₄O₅S 
• 1031857-99-4 C₂₂H₃₀F₂N₄O₃S 
• 1031858-00-0 C₂₈H₄₁BF₂N₄O₅S 
• 115416-38-1 N-(5-aminopentyl)-5-((3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazole-4-yl)pentanamide 

Relevant academic research and scientific papers

Fluorometric assay for tissue transglutaminase-mediated transamidation activity

Herein, we report the development of a direct discontinuous fluorometric transamidation assay for determining tissue transglutaminase (TG2) activity. In the assay reaction, TG2 catalyzes the formation of a biotin-fluorophore conjugate, using a fluorescent, high affinity γ-glutamyl donor substrate and a biotinylated amine as a γ-glutamyl acceptor substrate. After the reaction, the conjugate is fixed on streptavidin-coated beads and excess substrate is washed away, allowing the transamidation activity to be quantified by fluorescence measurement. This method was used to detect the activity of as little as 0.6 mU of purified TG2, and can be used for detection of activity from crude cellular lysates. Furthermore, this assay can be used for screening potential inhibitors and synthetic substrates, the latter of which was demonstrated herein.

BIOPROBES FOR LYSYL OXIDASES AND USES THEREOF

The present invention relates to novel bioprobes which are capable of binding to certain amine oxidase enzymes. These bioprobes are useful in methods of detecting and determining the concentration of certain amine oxidase enzymes in a sample as well as in methods for the quantitative assessment of inhibition of certain amine oxidases.

PHOTOPROXIMITY PROFILING OF PROTEIN-PROTEIN INTERACTIONS IN CELLS

Photoactive probes and probe systems for detecting biological interactions are described. The photoactive probes include probes that combine both photocleavable and photoreactive moieties. The photoactive probe systems can include a first probe comprising a photocatalytic group and a second probe comprising a group that can act as a substrate for the reaction catalyzed by the photocatalytic group. The probes and probe systems can also include groups that can specifically bind to a binding partner on a biological entity of interest and a detectable group or a precursor thereof. The probes and probe systems can detect spatiotemporal interactions of proteins or cells. In some embodiments, the interactions can be detected in live cells. Also described are methods of detecting the biological interactions.

Design, synthesis, antitumor activities and biological studies of novel diaryl substituted fused heterocycles as dual ligands targeting tubulin and katanin

Microtubule is one of the important targets for cancer treatment. A novel class of diaryl substituted imidazo[4,5-c]pyridin-2-ones and imidazo[4,5-c]pyridines were designed based on combination principles by merging the structures of β-lactams and purine-type compounds known as tubulin polymerization inhibitor and katanin activity up-regulator, respectively. Their antitumor activities were evaluated in vitro and the mechanism was elucidated, leading to the identification of 1,6-diaryl-1H-imidazo[4,5-c]pyridin-2(3H)-one 20b as the first bifunctional agent that can target both tubulin and katanin simultaneously. The in vivo assays verified that compound 20b significantly inhibited xenograft tumor growth with good pharmacokinetic characteristics, demonstrating a promising potential for further development into anti-tumor drug candidates with a unique mechanism of dual-targeting microtubule.

An improved synthesis of a fluorophosphonate-polyethylene glycol-biotin probe and its use against competitive substrates

The fluorophosphonate (FP) moiety attached to a biotin tag is a prototype chemical probe used to quantitatively analyze and enrich active serine hydrolases in complex proteomes in an approach called activity-based protein profiling (ABPP). In this study we have designed a novel synthetic route to a known FP probe linked by polyethylene glycol to a biotin tag (FP-PEG-biotin). Our route markedly increases the efficiency of the probe synthesis and overcomes several problems of a prior synthesis. As a proof of principle, FP-PEG-biotin was evaluated against isolated protein mixtures and different rat-tissue homogenates, showing its ability to specifically target serine hydrolases. We also assessed the ability of FP-PEG-biotin to compete with substrates that have high enzyme turnover rates. The reduced protein-band intensities resulting in these competition studies demonstrate a new application of FP-based probes seldom explored before.

Development of biotin-avidin technology to investigate okadaic acid-promoted cell signaling pathway

Four biotin conjugates of okadaic acid were synthesized for evaluating their interactions with protein phosphatase 2A (PP2A) by surface plasmon resonance (SPR). C7-biotinylated okadaic acid exhibited the strongest binding affinity to the enzyme, while Cl-biotinylated derivative was devoid of affinity. C24- or C27-biotinylated okadaic acid showed moderate affinity to the enzyme. In the wake of this finding, a biotinyl photoaffinity probe was introduced into 7-OH of okadaic acid. Photoaffinity labeling followed by SDS-PAGE analysis indicated that the okadaic acid derivative clearly labeled PP2A. Furthermore, three proteins were also labeled in crude extracts of a marine sponge Halichondria okadai. All these results imply that the C7-biotin conjugate is a versatile reagent for biochemical studies of okadaic acid-binding proteins including PP2A. (C) 2000 Elsevier Science Ltd.

Direct observation of binding between biotinylated okadaic acids and protein phosphatase 2A monitored by surface plasmon resonance

Two biotin conjugates of okadaic acid were synthesized for evaluating their interactions with protein phosphatase 2A by surface plasmon resonance (SPR). C7-biotinylated okadaic acid revealed strong binding affinity to the enzyme, while C1-biotinylated derivative being devoid of affinity, implying that the C7-biotin conjugate is a useful tool for biochemical studies of protein phosphatase 2A.