81306-93-6

Upstream product

• 61040-22-0 N^β-benzyloxycarbonyl-N^α-Boc-(S)-β-aminoalanine methyl ester 
• 76387-70-7 (S)-3-amino-2-tert-butoxycarbonylaminopropionic acid 
• 501-53-1 benzyl chloroformate 
• 7536-55-2 N-tert-butyloxycarbonylasparagine 
• 123-91-1 1,4-dioxane 
• 159002-17-2 N^α-Boc-α,β-diaminopropionic acid 
• 73259-81-1 (R)-2-tert-butoxycarbonyl-3-aminopropionic acid 
• 7536-55-2 N-t-butyloxycarbonyl-D-asparagine 
• 24424-99-5 di-tert-butyl dicarbonate 
• 61177-01-3 2-amino-3-benzyloxycarbonylaminopropionic acid 
• 1885-14-9 phenyl chloroformate 
• 71749-02-5 N^β-Z-Dap-OMe*HCl 
• 65621-26-3 (S)-N,N'-dicarbobenzyloxy-2,3-diaminopropanoic acid 
• 1025826-61-2 C₁₅H₂₄N₄O₇ 

Downstream Products

• 1632153-79-7 (S)-benzyl ((3,6-dioxopiperazin-2-yl)methyl)carbamate 
• 1632153-84-4 (S)-di-tert-butyl 3-((((benzyloxy)carbonyl)amino)methyl)-2,5-dioxopiperazine-1,4-dicarboxylate 
• 1653959-81-9 C₁₅H₂₁N₃O₅*C₂HF₃O₂ 
• 1653959-67-1 Boc-Dap(Z)-Gly-OEt 
• 61040-22-0 N^β-benzyloxycarbonyl-N^α-Boc-(R)-β-aminoalanine methyl ester 
• 915714-31-7 (S)-2-amino-3-(N'-Z-amino)propan-1-ol trifluoroacetic acid salt 
• 1296138-84-5 C₂₅H₃₇N₃O₈ 
• 1296138-83-4 YP-367 
• 957135-12-5 methyl (5S,8S,10aR)-5-[(tert-butoxycarbonyl)amino]-6-oxo-decahydro-1H-pyrrolo[1,2-a][1,5]diazocine-8-carboxylate 
• 61040-20-8 (S)-methyl 3-amino-2-((tert-butoxycarbonyl)amino)propanoate 
• 1429913-70-1 benzyl tert-butyl (3-hydroxypropane-1,2-diyl)biscarbamate 
• 675601-04-4 3-amino-N²-(tert-butoxycarbonyl)-N-methylalaninamide 

Relevant academic research and scientific papers

LINKING AMINO ACID SEQUENCES, MANUFACTURING METHOD THEREOF, AND USE THEREOF

This invention provides compositions comprising linked amino acid sequences, pharmaceutical compositions comprising linked amino acid sequences, and methods of making thereof. This invention also provides methods of delivering said compositions to subjects and methods of treating various disorders and diseases using the said compositions.

2-OXOIMIDAZOLIDINE-4-CARBOXAMIDES AS NAV1.8 INHIBITORS

Novel compounds of the structural formula (I), and the pharmaceutically acceptable salts thereof, are inhibitors of Nav1.8 channel activity and may be useful in the treatment, prevention, management, amelioration, control and suppression of diseases mediated by Nav1.8 channel activity. The compounds of the present invention may be useful in the treatment, prevention or management of pain disorders, cough disorders, acute itch disorders, and chronic itch disorders.

THERAPEUTIC COMPOUNDS AND METHODS

Disclosed herein are compounds of formula I: (I) or pharmaceutically acceptable salts thereof, wherein R1, R2, and R3 may any of the values defined herein, as well as compositions comprising such compounds. Also disclosed are methods for treating diseases including neurodegenerative disorders such as Parkinson's Disease and Alzheimer's Disease.

KCNT1 INHIBITORS AND METHODS OF USE

The present invention is directed to, in part, compounds and compositions useful for preventing and/or treating a neurological disease or disorder, a disease or condition relating to excessive neuronal excitability, and/or a gain-of-function mutation in a gene (e.g., KCNT1). Methods of treating a neurological disease or disorder, a disease or condition relating to excessive neuronal excitability, and/or a gain-of-function mutation in a gene such as KCNT1 are also provided herein.

A short, rigid linker between pyrene and guanidiniocarbonyl-pyrrole induced a new set of spectroscopic responses to the ds-DNA secondary structure

A novel pyrene-guanidiniocarbonyl-pyrrole dye, characterised by a short, rigid linker between the two chromophores, interacts strongly with ds-DNA but only negligibly with ds-RNA. Under neutral conditions the dye shows strong selectivity toward AT-DNA (with respect to GC-DNA). Binding is accompanied by a specific ICD band at 350 nm and fluorescence quenching for all DNAs/RNAs studied. At pH 5 the affinity of the dye is reversed, now favouring GC-DNA over AT-DNA. A strong emission increase for AT-DNA is observed but with quenching for GC-DNA.

A diversity-oriented synthesis strategy enabling the combinatorial-type variation of macrocyclic peptidomimetic scaffolds

Macrocyclic peptidomimetics are associated with a broad range of biological activities. However, despite such potentially valuable properties, the macrocyclic peptidomimetic structural class is generally considered as being poorly explored within drug discovery. This has been attributed to the lack of general methods for producing collections of macrocyclic peptidomimetics with high levels of structural, and thus shape, diversity. In particular, there is a lack of scaffold diversity in current macrocyclic peptidomimetic libraries; indeed, the efficient construction of diverse molecular scaffolds presents a formidable general challenge to the synthetic chemist. Herein we describe a new, advanced strategy for the diversity-oriented synthesis (DOS) of macrocyclic peptidomimetics that enables the combinatorial variation of molecular scaffolds (core macrocyclic ring architectures). The generality and robustness of this DOS strategy is demonstrated by the step-efficient synthesis of a structurally diverse library of over 200 macrocyclic peptidomimetic compounds, each based around a distinct molecular scaffold and isolated in milligram quantities, from readily available building-blocks. To the best of our knowledge this represents an unprecedented level of scaffold diversity in a synthetically derived library of macrocyclic peptidomimetics. Cheminformatic analysis indicated that the library compounds access regions of chemical space that are distinct from those addressed by top-selling brand-name drugs and macrocyclic natural products, illustrating the value of our DOS approach to sample regions of chemical space underexploited in current drug discovery efforts. An analysis of three-dimensional molecular shapes illustrated that the DOS library has a relatively high level of shape diversity.

2-PYRIDYL CARBOXAMIDE-CONTAINING SPLEEN TYROSINE KINASE (SYK) INHIBITORS

The invention provides certain 2-pyridyl carboxamide-containing compounds of the Formula (I) or pharmaceutically acceptable salts thereof, wherein A and B are as defined herein. The invention also provides pharmaceutical compositions comprising such compounds, and methods of using the compounds for treating diseases or conditions mediated by Spleen Tyrosine Kinase (Syk) kinase.

Aminomethylene peptide nucleic acid (am -PNA): Synthesis, regio-/stereospecific DNA binding, and differential cell uptake of (α/γ, R / S) am- PNA analogues

Inherently chiral, cationic am-PNAs having pendant aminomethylene groups at α(R/S) or γ(S) sites on PNA backbone have been synthesized. The modified PNAs are shown to stabilize duplexes with complementary cDNA in a regio- and stereo-preferred manner with γ(S)-am PNA superior to α(R/S)-am PNAs and α(R)-am PNA better than the α(S) isomer. The enhanced stabilization of am-PNA:DNA duplexes is accompanied by a greater discrimination of mismatched bases. This seems to be a combined result of both electrostatic interactions and conformational preorganization of backbone favoring the cDNA binding. The am-PNAs are demonstrated to effectively traverse the cell membrane, localize in the nucleus of HeLa cells, and exhibit low toxicity to cells.

PNAs grafted with (α/γ, R/S)-aminomethylene pendants: Regio and stereo specific effects on DNA binding and improved cell uptake

PNAs grafted with cationic aminomethylene (am) pendants on the backbone at the glycyl (α) or ethylenediamine (γ) segments show regio (α/γ) and stereochemistry (R/S) dependent binding with complementary DNA. These are efficiently taken up by cells, with γ(S-am) aeg-PNA being the best in all properties.

Inhibition of glyoxalase I: The first low-nanomolar tight-binding inhibitors

A series of rational modifications to the structure of known S-(N-aryl-N-hydroxycarbamoyl)glutathione-based glyoxalase I inhibitors culminated in the discovery of the first single-digit nanomolar inhibitor. This study makes available key information about possible means to address the issues of metabolic instability, low potency, and synthetic complexicity that have plagued the area of glyoxalase I inhibition. Knowledge garnered from this study has implications in the design of inhibitors with higher conformational definition and lower peptidic character.