41324-69-0

Usage

Uses

Used in Pharmaceutical Research and Development:
Boc-Ile-Pro-OH is utilized as a key building block in the synthesis of complex peptides and proteins for various pharmaceutical applications. Its role in facilitating selective deprotection and coupling reactions is vital for the production of new drugs and therapeutic proteins.
Used in Biochemical Research:
In the field of biochemistry, Boc-Ile-Pro-OH serves as an essential component for studying peptide and protein structures, functions, and interactions. Its presence in peptide synthesis allows researchers to explore the properties and potential applications of newly synthesized compounds.
Used in Peptide Synthesis:
Boc-Ile-Pro-OH is employed as a fundamental component in peptide synthesis, where its protective Boc group ensures the selective deprotection and coupling of amino acids. This selective process is crucial for the successful synthesis of desired peptide sequences with specific biological activities.
Used in Drug Design and Development:
Boc-Ile-Pro-OH contributes to the design and development of new drugs by providing a versatile building block for the creation of bioactive peptides and proteins. Its presence in the synthesis process allows for the exploration of novel drug candidates with potential therapeutic effects.

Upstream product

• 3392-08-3 N-(tert-butoxy)carbonyl-L-isoleucine N-hydroxysuccinimide ester 
• 147-85-3 L-proline 
• 13139-16-7 N-(tert-butyloxycarbonyl)-L-isoleucine 
• 41324-66-7 H-Pro-OBzl 
• 2577-48-2 methyl (2S)-pyrrolidine carboxylate 
• 74257-99-1 (S)-benzyl 1-((2S,3S)-2-(tert-butoxycarbonylamino)-3-methylpentanoyl)pyrrolidine-2-carboxylate 
• 68856-94-0 (S)-methyl 1-((2S,3S)-2(tert-butoxycarbonylamino)-3-mehylpentanoyl)pyrrolidine-2-carboxylate 

Downstream Products

• 136138-72-2 Boc-Ile-Pro-Tyr-OBzl 
• 37462-92-3 Ile-Pro 
• 852333-15-4 Boc-Ile-Pro-Pro-Tyr-OMe 
• 324775-53-3 N-benzoyl-L-isoleucyl-L-proline 
• 663923-84-0 1-(tert-butoxycarbonylamino)-3-(N-benzoyl-L-isoleucyl-L-prolyl-amino)propane 
• 140119-27-3 H-Ile-Pro-OPac * p-toluenesulphonic acid 
• 852333-18-7 Boc-Ile-Pro-Pro-Tyr-Val-Pro-Leu-Ile-OMe 
• 874337-86-7 Boc-Ile-Pro-Pro-Tyr-OH 
• 181121-70-0 Boc-Ile-Pro-Glu(OBzl)-Tyr(Cl₂Bzl)-Tyr(Cl₂Bzl)-OPac 
• 140119-25-1 Boc-Ile-Pro-OPac 

Relevant academic research and scientific papers

Total Synthesis of Reniochalistatin e

Reniochalistatin E (1) is one of the five related cyclic peptides isolated from the marine sponge Reniochalina stalagmitis. The discovery of these compounds resulted from a screening program directed toward the identification of proline-rich bioactive compounds. Reniochalistatin E is the only member of the family to possess a tryptophan amino acid residue. Given the cytotoxicity observed for 1, efforts were directed toward developing a synthetic route to 1. The first total synthesis of 1 has been accomplished in a 15-step route in an overall 5.0% yield. The synthetic sample of reniochalistatin E was shown to have similar activity toward HeLa and RPMI-8226 cell lines compared to the natural sample, with IC50 values of 16.9 vs 17.3 μM and 4.5 vs 4.9 μM, respectively. Interestingly, both of the fully deprotected octapeptides constructed toward the synthesis of reniochalistatin E were shown to have cytotoxicity. The route provides a means to probe the structure-activity relationship of 1 and further biological investigations.

Towards the total synthesis of MKN-349A

Attempts towards the total synthesis of MKN-349A and synthesis and characterization of a new and symmetric by-product, cyclooctapeptide is described. The characterization of the cyclooctapeptide is established using advanced NMR and MALDI studies.

Synthetic studies on cyclic octapeptides: Yunnanin F and Hymenistatin

Two biologically active cyclic peptides, Yunnanin F 8 and Hymenistatin 16 were synthesized and the structures were established on the basis of analytical, IR, NMR and mass spectral data. The newly synthesized compounds were screened for their antimicrobia

New cyanopeptide-derived low molecular weight inhibitors of trypsin-like serine proteases

This paper deals with the design, syntheses, and inhibition tests of new low molecular weight thrombin inhibitors utilizing cyanopeptides, the secondary metabolites of cyanobacteria with interesting biological activities, as new lead structures. Starting with aeruginosin 98-B (1) as a lead structure, we have developed and synthesised new, selective acting inhibitors of serine proteases (RA-1005 and RA-1009), which are suitable targets for further structure-activity studies.

Synthesis and kinetics of oxidation of some dipeptides with anodically generated manganese(III) sulphate: Mechanistic study

Dipeptides (DP) namely phenylalanyl-proline (Phe-Pro), isoleucyl-proline (Ile-Pro), and leucyl-proline (Leu-Pro) were synthesized by classical solution method and characterized. The kinetics of oxidation of these DP by Mn(III) have been studied in the presence of sulphate ions in acidic medium at 26°C. The reaction was followed spectrophotometrically at λmax = 500 nm. A first-order dependence of rate on both [Mn(III)]0 and [DP]0 was observed. The rate is independent of the concentration of reduction product, Mn(II), and hydrogen ions. The effects of varying dielectric constant of the medium and addition of anions such as sulphate, chloride, and perchlorate were studied. The activation parameters have been evaluated using Arrhenius and Eyring plots. The oxidation products were isolated and characterized. A mechanism involving the reaction of DP with Mn(III) in the rate-limiting step is suggested.

LARGE-SCALE SYNTHESIS OF ANTICOAGULANT DECAPEPTIDE MDL 28050

A solution phase synthesis of the anticoagulant decapeptide Suc-Tyr-Glu-Pro-Ile-Pro-Glu-Glu-Ala-Cha-D-Glu-OH ( 1, MDL 28050) on a large scale is decribed.Our strategy employed in the 24-step total synthesis relies on a convergent approach.The basic feature is the preparation and the coupling of two protected pentapeptides, 2 and 3.Several key intermediates were purified by crystallizations including the protected decapeptide 21.Only a single purification required preparative HPLC.Using this synthetic route, we prepared 98percent pure final product on a 40-g scale.The overall yield of this process is about 20percent.

Synthesis of immunostimulating hexapeptide corresponding to sequence 54-59 of human β-casein

Synthesis of immunostimulating hexapeptide Val-Glu-Pro-Ile-Pro-Tyr corresponding to human β-casein fragment 54-59 has been achieved.Starting from Tyr-OBzl, the protected hexapeptide Z-Val-Glu(OBzl)-Pro-Ile-Pro-Tyr-OBzl (6) has been obtained by stepwise ad