99532-43-1

Upstream product

• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 18942-49-9 Boc-D-Phe-OH 
• 2592-95-2 benzotriazol-1-ol 
• 24424-99-5 di-tert-butyl dicarbonate 
• 63-91-2 L-phenylalanine 

Downstream Products

• 104706-65-2 Boc-Phe-Asn-Glu(Bzl)-Asn-Met-Ala-Tyr(Bzl)-OMe 
• 88463-18-7 (S)-2-[(tert-butoxycarbonyl)amino]-3-phenylpropionamide 
• 530103-25-4 N-tBOC-L-Phe-1-anthraquinonylhydrazide 
• 191793-79-0 C₂₀H₂₈N₂O₆ 
• 530103-26-5 N-tBOC-D-Phe-1-anthraquinonylhydrazide 
• 530103-33-4 N-tBOC-L-Ala-L-Ala-D-Phe-1-anthraquinonylhydrazide 
• 58569-55-4 met-enkephalin 
• 61543-22-4 Boc-Phe-Met-OBzl 
• 1364570-17-1 17β-(Arg-Gly-Asp-Phe-amido)-11-α-hydroxyandrost-1,4-diene-3-one 
• 1364570-66-0 17β-[Boc-Arg(Tos)-Gly-Asp(OBzl)-Phe-amido]-11α-hydroxyandrost-1,4-diene-3-one 
• 1364570-52-4 C₄₄H₅₅N₃O₈ 
• 1364570-46-6 17β-[Boc-Asp(OBzl)-Val-amido]-11α-hydroxyandrost-1,4-diene-3-one 
• 1364570-41-1 17β-[Boc-Asp(OBzl)-Ser(Bzl)-amido]-11α-hydroxyandrost-1,4-diene-3-one 

Relevant academic research and scientific papers

Synthesis of Met-enkephalin by solution-phase peptide synthesis methodology utilizing para-toluene sulfonic acid as N-terminal masking of l-methionine amino acid

The Met-enkephalin, Tyr-Gly-Gly-Phe-Met, was synthesized by the solution-phase synthesis (SPS) methodology employing -OBzl group as carboxyls' protection, while the t-Boc groups were employed for the N-terminal α-amines' protection for the majority of the amino acids of the pentapeptide sequence. The l-methionine (l-Met) amino acid was used as PTSA.Met-OBzl obtained from the simultaneous protection of the α-amino, and carboxyl group with para-toluene sulfonic acid (PTSA) and as-OBzl ester, respectively in a C-terminal start of the 2?+?2?+?1 fragments condensation convergent synthetic approach. The protection strategy provided a short, single-step, simultaneous, orthogonal, nearly quantitative, robust, and stable process to carry through the protected l-methionine and l-phenylalanine coupling without any structural deformities during coupling and workups. The structurally confirmed final pentapeptide product was feasibly obtained in good yields through the current approach.

Novel nano-materials, RGD-tetrapeptide-modified 17β-amino-11α- hydroxyandrost-1,4-diene-3-one: Synthesis, self-assembly based nano-images and in vivo anti-osteoporosis evaluation

To find novel nano-materials with anti-osteoporosis activity and without side effects three novel anti-osteoporosis active amphiphiles, 17β-(RGD-AA-amido)-11α-hydroxyandrost-1,4-diene-3-one (5a: AA = Ser, 5b: AA = Val, 5c: AA = Phe), were constructed by coupling the bone resorption inhibiting active RGD-peptides and anti-osteoporosis active 17β-amino- 11α-hydroxyandrost-1,4-diene-3-one. In the solid state 5a, 5b and 5c exist as dispersed globes of 300 nm-14 μm in diameter, dispersed eggs of 110 nm-19 μm in diameter and beads of 238 nm-22 μm in diameter, respectively. In ultrapure water 1.1 μM of 5a, 5b and 5c form nano-globes of 33-400 nm, 16-278 nm and 54-187 nm in diameter, respectively. At an oral dose of 110 nmol kg -15a-c effectively inhibited mice from developing osteoporosis. In contrast to estradiol, 5a-c did not induce mice to develop endometrial hyperplasia and thrombus.

(3S)-N-(l-Aminoacyl)-1,2,3,4-tetrahydroisoquinolines, a class of novel antithrombotic agents: Synthesis, bioassay, 3D QSAR, and ADME analysis

To increase antithrombotic activity, 3S-tetrahydroisoquinoline-3-carboxylic acid (1) was modified with natural amino acids to form 19 novel dipeptide analogs, 3S-tetrahydroisoquinoline-3-carboxyamino acids (5a-s), targeting the intestinal peptide transport system. In vitro assay of 5a-s indicated that their potencies for inhibiting adenosine diphosphate (ADP), arachidonic acid (AA), platelet-activating factor (PAF), and thrombin (TH)-induced platelet aggregations were higher than that of 1. Additionally, in vivo assay of 5a-s indicated that their potencies for inhibiting thrombogenesis in rats were also higher than that of 1. Among the candidates, 5h with Ser attachment showed the most impressive features for further development. According to molecular field analysis based Cerius2 QSAR module, two equations (r, 0.961 and 0.988) correlating the structures with both in vitro and in vivo activities of 5a-s were established. ADMET calculations predict higher intestinal absorption for compounds 5a-s. Further investigation with 5h as a lead compound is underway.

Design, synthesis, inhibitory activity, and SAR studies of pyrrolidine derivatives as neuraminidase inhibitors

A series of pyrrolidine derivatives were synthesized and evaluated for their ability to inhibit neuraminidase (NA) of influenza A virus (H3N2). All compounds were synthesized in good yields starting from commercially 4-hydroxy-l-proline using a suitable synthetic strategy. These compounds showed potent inhibitory activity against influenza A neuraminidase. Within this series, five compounds, 6e, 9c, 9e, 9f, and 10e, have good potency (IC50 = 1.56-2.71 μM) which are compared to that the NA inhibitor Oseltamivir (IC50 = 1.06 μM), and could be used as lead compoundS in the future.

Tripeptide probes for tripeptidyl protease I production via gene transfer

Tripeptides derived from 5-chloroanthraquinone hydrazide and anthraquinone hydrazide have been prepared as potential reagents to probe cellular expression of tripeptidyl protease I (TPP-I). Attempted chemical synthesis of Gly-L-Pro-L-Ala-chloroanthraquino

Polymer-Assisted Solution-Phase (PASP) parallel synthesis of an α-ketothiazole library as tissue factor VIIa inhibitors

A solution-phase synthesis of an α-ketothiazole library of the general form D-Phe-L-AA-L-Arg-α-ketothiazole is described. The five-step synthesis is accomplished using a combination of polymeric reagents and polymer-assisted solution-phase purification protocols, including reactant-sequestering resins, reagent-sequestering resins, and tagged reagents. The multi-step synthesis affords the desired α-ketothiazole products in excellent purities and yields. A variety of L-amino acid inputs were used to probe the S2 pocket of the tissue factor (TF) VIIa enzyme to influence both potency and selectivity. An X-ray crystal structure of compound 10e bound to the TF/VIIa complex was obtained that explains the observed selectivity. The α-ketothiazoles were found to be potent, reversible-covalent inhibitors of tissue factor VIIa, with some analogues demonstrating selectivity versus thrombin.

Polymer-assisted solution-phase library synthesis and crystal structure of α-ketothiazoles as tissue factor VIIa inhibitors

A solution-phase synthesis of an α-ketothiazole library of the general form D-Phe-L-AA-Arg-α-ketothiazole is described. The five-step synthesis is accomplished using a combination of polymeric reagents and polymer-assisted solution-phase purification concepts, including reactant-sequestering resins, reagent-sequestering resins, and tagged reagents. The multistep synthesis affords desired α-ketothiazole products in excellent purities and yields. A variety of L-amino acid inputs were used to probe the S2 pocket of tissue Factor VIIa enzyme to influence both potency and selectivity. An X-ray crystal structure of compound 10k bound to the TF/VIIa complex was obtained that explains the observed selectivity. The α-ketothiazoles were found to be potent, reversible-covalent inhibitors of tissue Factor VIIa, with some analogues demonstrating selectivity over thrombin.

A one-step synthesis of aminosuccinyl peptides

Aminosuccinyl peptides were obtained by acylation of alpha-amino esters with tert-butyloxycarbonyl-L- and D-aspartic acids in the presence of N- ethyl-N'-(3-dimethylaminopropyl)carbodiimide and N-hydroxybenzotriazole.

Biological active acridine derivatives. Part 4: Synthesis and antiviral activity of some bis-acridinylated diamides

Nine bis-acridine derivatives have been synthesized in search of structures with antiviral properties. Synthesis of target compounds was provided by a standard peptide-like coupling procedure using aliphatic diamines and protected amino acids following pr