26055-05-0Relevant articles and documents
Hydrolysis of polypeptide esters with tetrabutylammonium hydroxide
Abdel-Magid,Cohen,Maryanoff,Shah,Villani,Zhang
, p. 3391 - 3394 (1998)
Tetrabutylammonium hydroxide is effective in hydrolysis of polypeptide esters to the corresponding acids with minimum racemization of the stereogenic centers at the α-positions. It is especially effective in hydrolysis of non-polar polypeptide esters that
Redox-triggered changes in the self-assembly of a ferrocene-peptide conjugate
Adhikari, Bimalendu,Kraatz, Heinz-Bernhard
, p. 5551 - 5553 (2014/05/20)
Ultrasonication of a ferrocene conjugate of a short amyloid peptide (Aβ18-20) in toluene causes formation of an organogel, which undergoes dramatic structural changes upon oxidation from a nanofibrillar network to spherical micelles. This morphological change is redox-controlled and reversible. the Partner Organisations 2014.
α-N-Protected dipeptide acids: A simple and efficient synthesis via the easily accessible mixed anhydride method using free amino acids in DMSO and tetrabutylammonium hydroxide
Verardo,Gorassini
, p. 315 - 324 (2013/06/05)
The importance of dipeptides both in medicinal and pharmacological fields is well documented and many efforts have been made to find simple and efficient methods for their synthesis. For this reason, we have investigated the synthesis of α-N-protected dipeptide acids by reacting the easily accessible mixed anhydride of α-N-protected amino acids with free amino acids under different reaction conditions. The combination of TBA-OH and DMSO has been found to be the best to overcome the low solubility of amino acids in organic solvents. Under these experimental conditions, the homogeneous phase condensation reaction occurs rapidly and without detectable epimerization. The present method is also applicable to side-chain unprotected Tyr, Trp, Glu, and Asp but not Lys. This latter residue is able to engage two molecules of mixed anhydride giving the corresponding isotripeptide. Moreover, the applicability of this protocol for the synthesis of tri- and tetrapeptides has been tested. This approach reduces the need for protecting groups, is cost effective, scalable, and yields dipeptide acids that can be used as building blocks in the synthesis of larger peptides.
Synthesis of sansalvamide A peptidomimetics: Triazole, oxazole, thiazole, and pseudoproline containing compounds
Davis, Melinda R.,Singh, Erinprit K.,Wahyudi, Hendra,Alexander, Leslie D.,Kunicki, Joseph B.,Nazarova, Lidia A.,Fairweather, Kelly A.,Giltrap, Andrew M.,Jolliffe, Katrina A.,McAlpine, Shelli R.
, p. 1029 - 1051 (2012/02/15)
Peptidomimetic-based macrocycles typically have improved pharmacokinetic properties over those observed with peptide analogs. Described are the syntheses of 13 peptidomimetic derivatives that are based on active sansalvamide A structures, where these analogs incorporate heterocycles (triazoles, oxazoles, thiazoles, or pseudoprolines) along the macrocyclic backbone. The syntheses of these derivatives employ several approaches that can be applied to convert a macrocyclic peptide into its peptidomimetic counterpart. These approaches include peptide modifications to generate the alkyne and azide for click chemistry, a serine conversion into an oxazole, a Hantzsch reaction to generate the thiazole, and protected threonine to generate the pseudoproline derivatives. Furthermore, we show that two different peptidomimetic moieties, triazoles, and thiazoles, can be incorporated into the macrocyclic backbone without reducing cytotoxicity: triazole and thiazole.
Salts responsive nanovesicles through π-Stacking induced self-assembly of backbone modified tripeptides
Koley, Pradyot,Drew, Michael G.B.,Pramanik, Animesh
, p. 6747 - 6756 (2012/05/20)
A set of backbone modified peptides of general formula Boc-Xx-m-ABA-Yy-OMe where m-ABA is meta-aminobenzoic acid and Xx and Yy are natural amino acids such as Phe, Gly, Pro, Leu, Ile, Tyr and Trp etc., are found to self-assemble into soft nanovesicular st
Compounds for enzyme inhibition
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Page/Page column 23; 24, (2008/06/13)
Peptide-based compounds including heteroatom-containing, three-membered rings efficiently and selectively inhibit specific activities of N-terminal nucleophile (Ntn) hydrolases associated with the proteasome. The peptide-based compounds include an epoxide
Structure-based design, synthesis, and biological evaluation of irreversible human rhinovirus 3C protease inhibitors. 2. Peptide structure- activity studies
Dragovich, Peter S.,Webber, Stephen E.,Babine, Robert E.,Fuhrman, Sheila A.,Patick, Amy K.,Matthews, David A.,Reich, Siegfried H.,Marakovits, Joseph T.,Prins, Thomas J.,Zhou, Ru,Tikhe, Jayashree,Littlefield, Ethel S.,Bleckman, Ted M.,Wallace, Michael B.,Little, Thomas L.,Ford, Clifford E.,Meador III, James W.,Ferre, Rose Ann,Brown, Edward L.,Binford, Susan L.,DeLisle, Dorothy M.,Worland, Stephen T.
, p. 2819 - 2834 (2007/10/03)
The structure-based design, chemical synthesis, and biological evaluation of various peptidederived human rhinovirus (HRV) 3C protease (3CP) inhibitors are described. These compounds are comprised of an ethyl propenoate Michael acceptor moiety and a tripeptidyl binding determinant. The systematic modification of each amino acid residue present in the binding determinant as well as the N-terminal functionality is described. Such modifications are shown to provide irreversible HRV-14 3CP inhibitors with anti-3CP activities (k(obs)/[I]) ranging from 60 to 280 000 M-1 s-1 and antiviral EC50's which approach 0.15 μM. An optimized inhibitor which incorporates several improvements identified by the structure-activity studies is also described. This molecule displays very rapid irreversible inhibition of HRV-14 3CP (k(obs)/[I] = 800 000 M-1 s-1) and potent antiviral activity against HRV-14 in cell culture (EC50 = 0.056 μM). A 1.9 A? crystal structure of an S-alkylthiocarbamate-containing inhibitor complexed with HRV-2 3CP is also detailed.
Comparative lipase-catalyzed hydrolysis of ethylene glycol derived esters. The 2-methoxyethyl ester as a protective group in peptide and glycopeptide synthesis
Gewehr, Markus,Kunz, Horst
, p. 1499 - 1510 (2007/10/03)
Comparison of the lipase-catalyzed cleavage of polar esters derived from ethylene glycol proved 2-methoxyethyl (ME) esters most favorable protecting groups for the carboxylic function of peptides and glycopeptides. They combine high substrate acceptance and iligh yields of hydrolysis with favorable physicochemical properties and advantageous solubility. The application of this polar ester as protecting group was extended to N-glycosylated amino acids and N-glycopeptides. The selective removal of ME esters by lipases was achieved under mild conditions (pH 7.0 and 37°C), leaving all other linkages including peptide bonds and other ester protecting groups unaffected.
Selective Enzymatic Removal of Protecting Groups: n-Heptyl Esters as Carboxy Protecting Functions in Peptide Synthesis
Braun, Peter,Waldmann, Herbert,Vogt, Walter,Kunz, Horst
, p. 165 - 170 (2007/10/02)
Amino acid heptyl (Hep) esters are accessible as generally crystalline hydro tosylates 3 from the amino acids by azeotropic esterification with 1-heptanol in high yields.They can be condensed with Z-, Boc-, and Aloc-protected amino acids to give the dipep
Cleavage of esters using carbonates and bicarbonates of alkali metals: Synthesis of thymopentin
Kaestle,Anwer,Audhya,Goldstein
, p. 327 - 330 (2007/10/02)
A novel method for hydrolysis of primary esters using aqueous alkali carbonates or bicarbonates and an alcohol as cosolvent is described. Several peptide esters, including a Cbz-Arg-Lys(Cbz)-Asp(OBzl)-Val-Tyr-OBzl (sequence corresponding to the active site of thymic immunoregulatory hormone, thymopoietin), were hydrolyzed to demonstrate the utility of this method.
