64088-62-6

Basic information

• Product Name: [D- TRP11 ]-NEUROTENSIN
• Synonyms: neurotensin, Tyr(11)-;neurotensin [D-Tyr11]
• CAS NO: 64088-62-6
• Molecular Formula: C78H121 N21 O20
• Molecular Weight: 1672.94
• Mol File: 64088-62-6.mol
• Article Data: 3

Chemical Properties

• Appearance: /
• CAS DataBase Reference: [D- TRP11 ]-NEUROTENSIN(CAS DataBase Reference)
• NIST Chemistry Reference: [D- TRP11 ]-NEUROTENSIN(64088-62-6)
• EPA Substance Registry System: [D- TRP11 ]-NEUROTENSIN(64088-62-6)

Safety Data

• Hazardous Substances Data: 64088-62-6(Hazardous Substances Data)

Usage

Description

[D-TRP11]-NEUROTENSIN is a synthetic analog of the neuropeptide neurotensin, which is involved in various physiological processes such as neurotransmission, cardiovascular regulation, and pain perception. This peptide exhibits potent analgesic effects in various animal models and also has antipsychotic properties. It has been investigated for its potential as a therapeutic agent for conditions like schizophrenia, chronic pain, and substance abuse due to its ability to modulate dopamine signaling.

Uses

Used in Pharmaceutical Industry:
[D-TRP11]-NEUROTENSIN is used as a therapeutic agent for the treatment of chronic pain due to its potent analgesic effects in animal models. It offers a potential alternative to conventional pain management therapies.
[D-TRP11]-NEUROTENSIN is also used as an antipsychotic agent for the treatment of schizophrenia. Its antipsychotic properties make it a promising candidate for managing the symptoms of this mental disorder.
Additionally, [D-TRP11]-NEUROTENSIN is used as a potential treatment for addiction and substance abuse. Its ability to modulate dopamine signaling suggests that it may help in managing cravings and reducing the risk of relapse in individuals struggling with addiction.
Furthermore, [D-TRP11]-NEUROTENSIN is used in research for its potential to modulate dopamine signaling, which may have implications for the development of new therapies for various neurological and psychiatric conditions.

Upstream product

• 35661-60-0 Fmoc-Leu-OH 
• 71989-31-6 Fmoc-Pro-OH 
• 71989-18-9 Fmoc-Glu(OtBu)-OH 
• 71989-23-6 Fmoc-Ile-OH 
• 71989-38-3 Fmoc-Tyr(tBu)-OH 
• 71989-26-9 Fmoc-Lys(tert-butoxycarbonyl) 
• 132388-59-1 L-Asn(Trt) 
• 98-79-3 L-Pyroglutamic acid 
• 187618-60-6 Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine 

Relevant articles and documents

Protein Modification at Tyrosine with Iminoxyl Radicals

Post-translational modifications (PTMs) of proteins are a biological mechanism for reversibly controlling protein function. Synthetic protein modifications (SPMs) at specific canonical amino acids can mimic PTMs. However, reversible SPMs at hydrophobic amino acid residues in proteins are especially limited. Here, we report a tyrosine (Tyr)-selective SPM utilizing persistent iminoxyl radicals, which are readily generated from sterically hindered oximes via single-electron oxidation. The reactivity of iminoxyl radicals with Tyr was dependent on the steric and electronic demands of oximes; isopropyl methyl piperidinium oxime 1f formed stable adducts, whereas the reaction of tert-butyl methyl piperidinium oxime 1o was reversible. The difference in reversibility between 1f and 1o, differentiated only by one methyl group, is due to the stability of iminoxyl radicals, which is partly dictated by the bond dissociation energy of oxime O-H groups. The Tyr-selective modifications with 1f and 1o proceeded under physiologically relevant, mild conditions. Specifically, the stable Tyr-modification with 1f introduced functional small molecules, including an azobenzene photoswitch, to proteins. Moreover, masking critical Tyr residues by SPM with 1o, and subsequent deconjugation triggered by the treatment with a thiol, enabled on-demand control of protein functions. We applied this reversible Tyr modification with 1o to alter an enzymatic activity and the binding affinity of a monoclonal antibody with an antigen upon modification/deconjugation. The on-demand ON/OFF switch of protein functions through Tyr-selective and reversible covalent-bond formation will provide unique opportunities in biological research and therapeutics.

NOVEL CROSS-LINKERS FOR OBTAINING STRUCTURE INFORMATION ON MOLECULE COMPLEXES

The present invention describes a novel cross-linker, a method for preparing one or more cross-linked biomolecules, biomolecular complexes of two or more biomolecules, a method for preparing cross-linked fragments from such cross-linked biomolecules and/or biomolecular complexes, a method for cleavage and reduction of such cross-linked biomolecules and/or biomolecular complexes, a method for identifying cross-links in such cross-linked biomolecules and/or biomolecular complexes, as well as a method for determining relative amounts of cross-links in a biomolecule or biomolecular complex in two or more samples.