98482-70-3

Upstream product

• 98482-69-0 tert-butyl-(3S)-3-{[(benzyloxy)carbonyl]amino}-4-[methoxy(methyl)amino]-4-oxobutanoate 
• 146398-02-9 tert-butyl (S)-3-benzyloxycarbonylamino-4-hydroxybutyrate 
• 5545-52-8 Z-D(tBu)-OH 
• 3338-32-7 Z-Asp(OtBu)-OSu 

Downstream Products

• 98482-71-4 (benzyloxycarbonyl)-β-tert-butyl-L-aspartyl-ψ(CH2-NH)-L-phenylalanine amide 
• 194484-81-6 (S)-1-[(S)-2-((S)-2-Benzyloxycarbonylamino-3-tert-butoxycarbonyl-propylamino)-6-tert-butoxycarbonylamino-hexanoyl]-pyrrolidine-2-carboxylic acid tert-butyl ester 
• 281208-44-4 tert-butyl-(3S)-3-{[(benzyloxy)carbonyl]amino}-4-pentenoate 
• 195072-01-6 C₂₃H₂₆N₂O₆ 
• 1246261-52-8 C₁₈H₂₅NO₆S 
• 1246261-51-7 C₂₃H₂₇NO₆S 
• 142955-60-0 ((2S,3S)-2-{(S)-Hydroxy-[(S)-1-((S)-8-hydroxy-1-oxo-isochroman-3-yl)-3-methyl-butylcarbamoyl]-methyl}-5-oxo-tetrahydro-furan-3-yl)-carbamic acid benzyl ester 
• 1391707-53-1 C₁₇H₂₅NO₅ 
• 1215015-96-5 tert-butyl (S,E)-3-(benzyloxycarbonylamino)-6-oxo-6-phenylhex-4-enoate 
• 98482-72-5 (S)-3-Amino-4-((S)-1-carbamoyl-2-phenyl-ethylamino)-butyric acid tert-butyl ester; hydrochloride 
• 98482-73-6 (tert-butyloxycarbonyl)-L-leucyl-β-tert-butyl-L-aspartyl-ψ(CH2-NH)-L-phenylalanine amide 
• 147395-39-9 Ac-Tyr-Val-(R)-Ala-Asp(O^tBu)-H dimethyl acetal 
• 147395-39-9 Ac-Tyr-Val-Ala-Asp(O^tBu)-H dimethyl acetal 
• 769964-73-0 (S)-4-(5-Fluoro-2,3-dihydro-indol-1-yl)-3-[(S)-2-(3-methoxy-benzoylamino)-4,4-dimethyl-pentanoylamino]-butyric acid tert-butyl ester 

Relevant academic research and scientific papers

Total Synthesis of Originally Proposed and Revised Structure of Hetiamacin A

The first total synthesis of the originally proposed and correct structures of hetiamacin A has been accomplished via Wittig olefination and Sharpless asymmetric dihydroxylation reaction. These total syntheses culminated in the stereostructural confirmati

Total synthesis method of hetiamacin A

The invention relates to a total synthesis method of hetiamacin A. The method comprises the steps as follows: a compound (S)-3-((S)-1-amino-3-methylbutyl)-8-hydroxy 3,4-dibydro-isobenzopyran-1-ketone and a compound (2S,3S,4S)-2-amino-4-(carbobenzoxy amino

Efficient access to enantiopure γ4-amino acids with proteinogenic side-chains and structural investigation of γ4- asn and γ4-ser in hybrid peptide helices

Hybrid peptides composed of α- and β-amino acids have recently emerged as new class of peptide foldamers. Comparatively, γ- and hybrid γ-peptides composed of γ4-amino acids are less studied than their β-counterparts. However, recent investigations reveal that γ4-amino acids have a higher propensity to fold into ordered helical structures. As amino acid side-chain functional groups play a crucial role in the biological context, the objective of this study was to investigate efficient synthesis of γ4-residues with functional proteinogenic side-chains and their structural analysis in hybrid-peptide sequences. Here, the efficient and enantiopure synthesis of various N- and C-terminal free-γ4-residues, starting from the benzyl esters (COOBzl) of N-Cbz-protected (E)-α,β-unsaturated γ-amino acids through multiple hydrogenolysis and double-bond reduction in a single-pot catalytic hydrogenation is reported. The crystal conformations of eight unprotected γ4-amino acids (γ4-Val, γ4-Leu, γ4-Ile, γ4-Thr(OtBu), γ4-Tyr, γ4-Asp(OtBu), γ4- Glu(OtBu), and γ-Aib) reveals that these amino acids adopted a helix favoring gauche conformations along the central Cγi￡ Cβ bond. To study the behavior of γ4- residues with functional side chains in peptide sequences, two short hybrid γ-peptides P1 (Ac-Aib-γ4-Asn-Aib-γ4-Leu- Aib-γ4-Leu-CONH2) and P2 (Ac-Aib- γ4-Ser-Aib-γ4-Val-Aib-γ4-Val- CONH2) were designed, synthesized on solid phase, and their 12-helical conformation in single crystals were studied. Remarkably, the γ4-Asn residue in P1 facilitates the tetrameric helical aggregations through interhelical H bonding between the side-chain amide groups. Furthermore, the hydroxyl side-chain of γ4-Ser in P2 is involved in the interhelical H bonding with the backbone amide group. In addition, the analysis of 87 γ4-residues in peptide single-crystals reveal that the γ4-residues in 12-helices are more ordered as compared with the 10/12- and 12/14-helices. Copyright

Synthesis of threo-β-aminoalcohols from aminoaldehydes via chelation-controlled additions. Total synthesis of l-threo sphingosine and safingol

Chelation-controlled addition of organocuprates to N-carbamoyl aminoaldehydes, prepared from functionalized amino acids, generated predominately the threo-β-amino alcohol derivatives through chelation with the carbamoyl moiety. The carbamate group is a stronger chelating group than other potentially good chelators, for example ethers, esters, thioethers, and gives good diastereoselectivity with cuprates. Thus addition of lithium divinylcuprate to the aldehyde generated from the serine derivative 25 in the presence of extra copper for chelation afforded the threo compound 26 in 83% yield. Cross-metathesis and cleavage of the protecting groups furnished l-threo sphingosine 21. In addition the lyso-sphingolipid protein kinase C inhibitor, safingol, 22, was prepared from commercially available O-benzyl N-BOC serine 28 in six steps and 56% overall yield by this method.

Expanding the scope of PNA-encoded libraries: divergent synthesis of libraries targeting cysteine, serine and metallo-proteases as well as tyrosine phosphatases

Seven PNA-encoded combinatorial libraries targeting proteases and phosphatases with covalent reversible and irreversible mechanism-based inhibitors were prepared. The libraries were synthesized using modified PNA monomers, which dramatically increase the water solubility of the libraries in biologically relevant buffers. The libraries were shown to selectively inhibit targeted enzymes.

Synthesis and evaluation of arylaminoethyl amides as noncovalent inhibitors of cathepsin S. Part 3: Heterocyclic P3

A series of Nα-2-benzoxazolyl-α-amino acid-(arylaminoethyl)amides were identified as potent, selective, and noncovalent inhibitors of cathepsin S. Structure-activity relationships including strategies for modulating the selectivities among cathepsins S, K, and L, and in vivo pharmacokinetics are discussed. A X-ray structure of compound 3 bound to the active site of cathepsin S is also reported.

Arylaminoethyl amides as noncovalent inhibitors of cathepsin S. Part 2: Optimization of P1 and N-aryl

A systematic study of anilines led to the discovery of a metabolically robust fluoroindoline replacement for the alkoxy aniline toxicophore in 1. Investigations of the P1 pocket resulted in the discovery of a wide tolerance of functionality leading to the discovery of 11 as a potent and selective inhibitor of cathepsin S.

(Substituted)acyl dipeptidyl inhibitors of the ICE/ced-3 family of cysteine proteases

This invention is directed to novel (substituted)acyl dipeptidyl ICE/ced-3 family inhibitor compounds. The invention is also directed to pharmaceutical compositions containing these compounds, as well as the use of such compositions in the treatment of pa

Iodolactonization of 3-amino-4-pentenoic acid: a stereoselective synthesis of syn-γ-hydroxy-β-amino acids

The reaction of (S)-3-N-Cbz-4-pentenoic acid with iodine in acetonitrile in the presence of AgOTf gave the cis-iodo-lactone 6 in excellent yield and in a highly diastereoselective manner. The substitutions of the iodine in 6 by different Grignard reagents in the presence of CuI and the subsequent conversions into the functionalized syn-γ-hydroxy-β-amino acids have been investigated. By the above reaction sequence, (3S,4S)-3-amino-4-hydroxy-5-cyclohexyl pentanoic acid was synthesized with high enantioselectivity.

Synthesis of N-protected α-amino aldehydes from their morpholine amide derivatives

A new method for the synthesis of N-protected α-amino aldehydes was developed. N-Protected α-amino amides of morpholine were easily prepared and then reduced with LiAlH4 to produce clean N-protected α-amino aldehydes. This new scheme of synthesis can be used with Boc, Z and Fmoc amino-protecting groups.