21323-98-8

Upstream product

• 60876-70-2 4-tert-butoxybromobenzene 
• 79-10-7 acrylic acid 
• 138585-07-6 t-Butyl p-t-butoxyhydrocinnamate 
• 501-97-3 4-hydroxyphenylpropionic acid 
• 57699-45-3 p-tert-butoxybenzaldehyde 
• 155904-35-1 3-(4-tert-butoxy-phenyl)-acrylic acid 

Downstream Products

• 1400684-94-7 3-(4-(tert-butoxy)phenyl)-N-methoxy-N-methylpropanamide 
• 941293-00-1 3-(4-tert-butoxyphenyl)propionaldehyde 
• 1400685-19-9 (E)-benzyl 2-(4-(tert-butoxy)benzyl)but-2-enoate 
• 727716-46-3 3-(4-tert-butoxyphenyl)propionic acid benzyl ester 
• 1165738-62-4 3-(4-tert-butoxyphenyl)-N-(3-fluoro-4-(methylsulfonamido)benzyl)propanamide 
• 397883-78-2 4-(4-benzyl-2-oxo-oxazolidin-3-yl)-3-(4-tert-butoxy-benzyl)-N-(2,4-dimethoxy-benzyl)-N-methyl-4-oxo-butyramide 
• 326473-17-0 (4-S)-4-benzyl-3-[3-(4-tert-butoxyphenyl)-propionyl]-oxazolidin-2-one 
• 397883-85-1 (2S,3S)-2-[(S)-4-Benzyloxycarbonyl-2-((S)-4-benzyloxycarbonyl-2-{(R)-3-[4-(bis-benzyloxy-phosphoryloxy)-phenyl]-2-methylcarbamoylmethyl-propionylamino}-butyrylamino)-butyrylamino]-3-methyl-pentanoic acid benzyl ester 
• 397883-84-0 (2S,3S)-2-[(S)-4-Benzyloxycarbonyl-2-((S)-4-benzyloxycarbonyl-2-{(R)-3-[4-(bis-benzyloxy-phosphoryloxy)-phenyl]-2-dimethylcarbamoylmethyl-propionylamino}-butyrylamino)-butyrylamino]-3-methyl-pentanoic acid benzyl ester 
• 326473-19-2 (2R)-2-(4-tert-butoxybenzyl)-N-(2,4-dimethoxybenzyl)-N-methylsuccinamic acid benzyl ester 
• 397883-83-9 (2R)-2-[4-(bis-benzyloxy-phosphoryloxy)-benzyl]-N-methyl-succinamic acid 
• 397883-82-8 (2R)-2-[4-(bis-benzyloxy-phosphoryloxy)-benzyl]-N,N-dimethyl succinamic acid 
• 397883-76-0 [3R,4S]-4-(4-benzyl-2-oxo-oxazolidin-3-yl)-3-(4-tert-butoxybenzyl)-N,N-dimethyl-4-oxo-butyramide 

Relevant academic research and scientific papers

Modulating the selectivity of matriptase-2 inhibitors with unnatural amino acids

Matriptase-2, a type II transmembrane serine protease (TTSP), is expressed in the liver and regulates iron homeostasis via the cleavage of hemojuvelin. Matriptase-2 emerges as an attractive target for the treatment of conditions associated with iron overload, such as hemochromatosis or beta-thalassemia. Starting from the crystal structure of its closest homolog matriptase, we constructed a homology model of matriptase-2 in order to further optimize the selectivity of serine trap peptidomimetic inhibitors for matriptase-2 vs matriptase. Careful modifications of the P4, P3 and P2 positions with the help of unnatural amino acids led to a thorough understanding of Structure-Activity Relationship and a >60-fold increase in selectivity for matriptase-2 vs matriptase. Additionally, the introduction of unnatural amino acids led to significant increases in plasma stability. Such compounds represent useful pharmacological tools to test matriptase-2 inhibition in a context of iron overload.

Design strategies for the sequence-based mimicry of side-chain display in protein β-sheets by α/β-peptides

The sophistication of folding patterns and functions displayed by unnatural-backbone oligomers has increased tremendously in recent years. Design strategies for the mimicry of tertiary structures seem within reach; however, a general method for the mimicry of sheet segments in the context of a folded protein is an unmet need preventing realization of this goal. Previous work has shown that 1→1 α→β-residue substitutions at cross-strand positions in a hairpin-forming α-peptide sequence can generate an α/β-peptide analogue that folds in aqueous conditions but with a change in side-chain display relative to the natural sequence; this change would prevent application of single β-residue substitutions in a larger protein. Here, we evaluate four different substitution strategies based on replacement of αα dipeptide segments for the ability to retain both sheet folding encoded by a parent α-peptide sequence as well as nativelike side-chain display in the vicinity of the β-residue insertion point. High-resolution structure determination and thermodynamic analysis of folding by multidimensional NMR suggest that three of the four designs examined are applicable to larger proteins.

Design, synthesis, and biological evaluation of novel diarylalkyl amides as TRPV1 antagonists

We have developed a new class of diarylalkyl amides as novel TRPV1 antagonists. They exhibited potent 45Ca2+ uptake inhibitions in rat DRG neuron. In particular, the amide 59 was identified as a potent antagonist with IC50 of 57 nM. The synthesis and structure-activity relationship of the diarylalkyl amides are also described.

Calorimetric and structural studies of 1,2,3-trisubstituted cyclopropanes as conformationally constrained peptide inhibitors of Src SH2 domain binding

Isothermal titration calorimetry and X-ray crystallography have been used to determine the structural and thermodynamic consequences associated with constraining the pTyr residue of the pYEEI ligand for the Src Homology 2 domain of the Src kinase (Src SH2

Use of 1,2,3-trisubstituted cyclopropanes as conformationally constrained peptide mimics in SH2 antagonists

Novel conformationally constrained phosphotyrosine pseudopeptide derivatives of the tetrapeptide pY-E-E-I were prepared and evaluated as SH2 binding antagonists. (C) 2000 Elsevier Science Ltd.

Inhibitor of ribonucleotide reductase of herpes viruses

A series of substituted peptides have been found to possess antiviral potency - specifically against herpes viruses - by selectively inhibiting the viral ribonucleotide reductase enzyme.

Phlorethyl-β-alanyl-secretine

A radioiodinated phloretyl-β-alanyl-secretin, its salts and its protected derivatives. A process for the manufacture of a radioiodinated phloretyl-β-alanyl-secretin and/or a salt thereof which process involves reacting phloretyl-β-alanyl-secretin and/or a