K‐Oxyma: a Strong Acylation‐Promoting, 2‐CTC Resin‐Friendly Coupling Additive

Cherkupally, Prabhakar; Acosta, Gerardo; Nieto-Rodriguez, Lidia; Spengler, Jan; Rodríguez, Hortensia; Khattab, Sherine N.; El‐Faham, Ayman; Shamis, Marina; Luxembourg, Yoav; Prohens, Rafel; Subirós‐Funosas, Ramon; Alberício, Fernando

doi:10.1002/ejoc.201300777

Cited by 32 publications

(39 citation statements)

References 38 publications

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“…The efficency of using THF or ACN in solid-phase peptide synthesis was further tested in a longer synthesis of Aib 67 , Aib 68modified ACP decapeptide 10 model (H-Val-Gln-Aib 67 -Aib 68 -Ile-Asp-Tyr-Ile-Asn-Gly-NH 2 ). [34][35][36] To the best of our knowledge, 45 unmodified ACP decapeptide has frequently beenused fortestingnew protocols. 17,[37][38][39] In this study, two Aib residuesreplaced the two consecutive Ala residues in the normal ACP decapeptide in order to make it a more difficult sequence and as a result allow a clear observation of the effect of solvent 50 on the synthesis of a long peptide.Decapeptide 10 was manually assembledstepwise on Fmoc-RinkAmide-AM-ChemMatrix-resin by means of a 1-h coupling (except Aib-Aib where a 2-h double coupling was applied) with an excess of 3 equivalents of Fmocamino acid/additive/carbodiimide.…”

Section: Resultsmentioning

confidence: 99%

Peptide synthesis beyond DMF: THF and ACN as excellent and friendlier alternatives

et al. 2015

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To date, DMF has been considered as the only solvent suitable for peptide synthesis. Here we demonstrate the capacity of THF and ACN, which are friendlier solvents than DMF, to yield the product in higher purity than DMF. Using various peptide models, both THF and ACN reduced racemization in solution-phase and solid-phase synthesis when compared with DMF. Moreover, the use of ACN and THF in the solid-phase peptide synthesis of hindered peptides, such as Aib-enkephalin pentapeptide and Aib-ACP decapeptide, in combination with a complete polyethylene glycol resin (ChemMatrix), gave a better coupling efficiency than DMF.

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Section: Resultsmentioning

confidence: 99%

Peptide synthesis beyond DMF: THF and ACN as excellent and friendlier alternatives

et al. 2015

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“…As outlined in Scheme 2, the synthesis was started with the above-mentioned compound 6,w hich was first treated with piperidine to remove the Fmoc protecting groups,f ollowed by coupling with ad iisopropylcarbodiimide (DIC) pre-activated Fmoc amino acidr esidue. [12] Linear octapeptides 9 and 10 wereo btained by repeating the deprotection and coupling steps to generate as equence of eight amino acid residues, followed by removal of the support with 2% TFA. For synthesis of reniochalistatin E, the connection order of residues is assigned from l-Pro to l-Leu (VII).…”

Section: Resultsmentioning

confidence: 99%

Synthesis and Biological Evaluation of Reniochalistatins A–E and a Reniochalistatin E Analogue

Zhou

Sun

et al. 2018

ChemMedChem

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The total synthesis of reniochalistatins A-E, along with a reniochalistatin E analogue (inverso-E) was successfully achieved through Fmoc-based solid-phase peptide synthesis and subsequent macrolactamization with PyBOP and DIEA. The biological activities of these reniochalistatins and a key linear peptide intermediate were systematically evaluated. Among these seven synthesized compounds, linear reniochalistatin B was found to have potent activity against several cancer cell lines not shown by the cyclic reniochalistatin B counterpart. In addition, linear reniochalistatin B was found to have antitubercular activity (IC =1.4 μm). Inverso-E possesses increasing cytotoxicity against the HeLa and LNCaP cell lines after simple alternation of the sequence of amino acids in reniochalistatin E. The results of these studies provide a feasible method to further investigate the structure-activity relationships (SARs) of reniochalistatins A-E.

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“…OxymaPure was shown to be superior to HOBt in all cases, and in many cases it gave the same performance as HOAt 14,15. Furthermore, we have also described K‐Oxyma ( 7 ) as a potassium salt of 6 , which proved to be a good alternative, especially when acid‐sensitive solid supports, such as CTC resins, were used 16. More recently, our group reported 5‐(hydroxyimino)‐1,3‐dimethylpyrimidine‐2,4,6(1 H ,3 H ,5 H )‐trione (Oxyma‐B; 8 ) as a new additive for peptide synthesis 17.…”

Section: Introductionmentioning

confidence: 88%

Biocatalytic Performance of pH‐Sensitive Magnetic Nanoparticles Derived from Layer‐by‐Layer Ionic Self‐Assembly of Chitosan with Glucoamylase

Wang

Zhao

et al. 2013

Chemistry An Asian Journal

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Based on the characteristics of polycations of chitosan and glucoamylase, which are oppositely charged, they were successfully alternatingly deposited onto the surface of aldehyde-modified Fe3O4 nanoparticles by using a layer-by-layer ion exchange method to form magnetic carriers to construct multilayer films (designated as Fe3O4@(CS/GA)n). The (CS/GA)n film systems were endowed with the pH-dependent properties of chitosan as well as the catalytic activity of glucoamylase. The changes in weight loss and surface chemistry, morphology, and magnetic sensitivity were monitored and verified by UV/Vis spectroscopy, zeta potential, TEM, and a vibrating sample magnetometer. Subsequently, the influence of the number of bilayers, storage stability, pH, temperature, and reusability of Fe3O4@(CS/GA)5 biocatalysts on catalytic activity were investigated. The results from characterization and determination remarkably indicate that Fe3O4@(CS/GA)5 presents excellent catalytic activity, storage stability, pH stability, and reusability in comparison with free enzyme. Fe3O4@(CS/GA)5 retained >60% of its initial activity at 65 °C over 6 h; the optimum temperature and pH also increased to the ranges of 45-65 °C and 2.5-3.5, respectively, and only 27% activity was lost after 10 cycles. This new strategy simplifies the reaction protocol and improves encapsulation efficiency and catalytic activity for new potential applications in biotechnology.

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K‐Oxyma: a Strong Acylation‐Promoting, 2‐CTC Resin‐Friendly Coupling Additive

Cited by 32 publications

References 38 publications

Peptide synthesis beyond DMF: THF and ACN as excellent and friendlier alternatives

Peptide synthesis beyond DMF: THF and ACN as excellent and friendlier alternatives

Synthesis and Biological Evaluation of Reniochalistatins A–E and a Reniochalistatin E Analogue

Biocatalytic Performance of pH‐Sensitive Magnetic Nanoparticles Derived from Layer‐by‐Layer Ionic Self‐Assembly of Chitosan with Glucoamylase

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