1480-30-4Relevant academic research and scientific papers
Selective, on-resin N-methylation of peptide N-trifluoroacetamides
Turner, Rushia A.,Hauksson, Niels E.,Gipe, Jordan H.,Lokey, R. Scott
, p. 5012 - 5015 (2013)
Mild and efficient methods for site-specific methylation of peptide backbone amides are important tools for chemists seeking to modulate the pharmacokinetic properties of peptide drugs. The Mitsunobu reaction was used to selectively methylate N-trifluoroa
Active Controlled and Tunable Coacervation Using Side-Chain Functional α-Helical Homopolypeptides
Barun, Ehab,Bell, Alexandra G.,Deming, Timothy J.,Evans, Declan,Gharakhanian, Eric G.,Houk, K. N.,Scott, Wendell A.
supporting information, p. 18196 - 18203 (2021/11/12)
We report the development of new side-chain amino acid-functionalized α-helical homopolypeptides that reversibly form coacervate phases in aqueous media. The designed multifunctional nature of the side-chains was found to provide a means to actively control coacervation via mild, biomimetic redox chemistry as well as allow response to physiologically relevant environmental changes in pH, temperature, and counterions. These homopolypeptides were found to possess properties that mimic many of those observed in natural coacervate forming intrinsically disordered proteins. Despite ordered α-helical conformations that are thought to disfavor coacervation, molecular dynamics simulations of a polypeptide model revealed a high degree of side-chain conformational disorder and hydration around the ordered backbone, which may explain the ability of these polypeptides to form coacervates. Overall, the modular design, uniform nature, and ordered chain conformations of these polypeptides were found to provide a well-defined platform for deconvolution of molecular elements that influence biopolymer coacervation and tuning of coacervate properties for downstream applications.
Synthesis of chiral TFA-protected α-amino aryl-ketone derivatives with friedel-crafts acylation of α-amino acid n-hydroxysuccinimide ester
Tachrim, Zetryana Puteri,Oida, Kazuhiro,Ikemoto, Haruka,Ohashi, Fumina,Kurokawa, Natsumi,Hayashi, Kento,Shikanai, Mami,Sakihama, Yasuko,Hashidoko, Yasuyuki,Hashimoto, Makoto
supporting information, (2017/11/07)
Chiral N-protected α-amino aryl-ketones are one of the useful precursors used in the synthesis of various biologically active compounds and can be constructed via Friedel-Crafts acylation of N-protected α-amino acids. One of the drawbacks of this reaction
Use of N-trifluoroacetyl-protected amino acid chlorides in peptide coupling reactions with virtually complete preservation of stereochemistry
Jass, Paul A.,Rosso, Victor W.,Racha, Saibaba,Soundararajan, Nachimuthu,Venit, John J.,Rusowicz, Andrew,Swaminathan, Shankar,Livshitz, Julia,Delaney, Edward J.
, p. 9019 - 9029 (2007/10/03)
The use of protected amino acid chlorides for peptide coupling reactions has long been avoided due to the extensive racemization that commonly occurs during either the acid chloride formation or the coupling reaction itself. Conditions are described which
ENANTIOSELECTIVE SYNTHESES OF α-AMINO ACIDS FROM 10-SULFONAMIDO-ISOBORNYL ESTERS AND DI-t-BUTYL AZODICARBOXYLATE
Oppolzer, Wolfgang,Moretti, Robert
, p. 5541 - 5552 (2007/10/02)
Successive treatment of chiral esters 7 with LDA/Me3SiCl and di-t-butyl azodicarboxylate/TiCl4 and Ti(OiPr)4 gave N,N-di-t-butoxycarbonylhydrazinoesters 11 which on deacylation, hydrogenolysis, transesterification and acidic hydrolysis furnished (2S)-α-amino acid hydrochlorides 13 in good overall yields, high enantiomeric purity and with efficient recovery of the alcohol auxiliary 4.Experimental evidence for the configuration and conformation of the intermediate O-silyl ketene acetals 1 is provided.
Effect of N-trifluoroacetyl derivatives of amino acids and amino acid analogs on microbial antitumor screen
Otani,Briley
, p. 496 - 499 (2007/10/05)
Eighteen trifluoroacetyl derivatives of amino acids and of amino acid analogs were prepared and tested for growth-inhibitory activity. Of the compounds tested, the trifluoroacetyl derivatives of o-, m-, and p-fluorophenylalanine and β-3-thienylalanine showed modest activity; trifluoroacetyl derivatives of phenylalanine and of β-2-thienylalanine showed marginal activity. The activity exhibited by the active trifluoroacetyl compounds was equal to that noted for most active chloroacetyl derivatives reported previously, as judged by comparison of their activity with that of chloroacetyl-m-fluorophenylalanine. No reversal of inhibition was noted when a representative of these inhibitors was challenged with a corresponding natural metabolite, both as free amino acid and as a noninhibitory acylated compound.
