889670-02-4Relevant articles and documents
Nickel-Catalyzed Cross-Coupling of Amino-Acid-Derived Alkylzinc Reagents with Alkyl Bromides/Chlorides: Access to Diverse Unnatural Amino Acids
Gou, Fei-Hu,Ma, Ming-Jian,Wang, An-Jun,Zhao, Liang,Wang, Haoyang,Tong, Jie,Wang, Ze,Wang, Zhen,He, Chun-Yang
supporting information, p. 240 - 244 (2022/01/12)
Unnatural α-amino acids are important synthetic targets in the field of peptide science. Herein we report an efficient, versatile, and straightforward strategy for the synthesis of homophenylalanine derivatives via the nickel-catalyzed Csp3–Csp3 cross-coupling of (fluoro)benzyl bromides/chlorides with natural α-amino-acid-derived alkylzinc reagents. The current protocol features the advantages of a low-cost nickel catalyst system, synthetic convenience, and the tolerance of rich functionality and stereochemistry.
ELONGATION FACTOR 1-ALPHA INHIBITORS AND USES THEREOF
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Paragraph 0551-0554; 0598-0603, (2021/08/13)
Disclosed herein, inter alia, are compounds for inhibiting Elongation Factor 1-alpha and uses thereof.
Site-Selective Modification of Peptides and Proteins via Interception of Free-Radical-Mediated Dechalcogenation
Griffiths, Rhys C.,Smith, Frances R.,Long, Jed E.,Williams, Huw E. L.,Layfield, Robert,Mitchell, Nicholas J.
supporting information, p. 23659 - 23667 (2020/10/21)
The development of site-selective chemistry targeting the canonical amino acids enables the controlled installation of desired functionalities into native peptides and proteins. Such techniques facilitate the development of polypeptide conjugates to advance therapeutics, diagnostics, and fundamental science. We report a versatile and selective method to functionalize peptides and proteins through free-radical-mediated dechalcogenation. By exploiting phosphine-induced homolysis of the C?Se and C?S bonds of selenocysteine and cysteine, respectively, we demonstrate the site-selective installation of groups appended to a persistent radical trap. The reaction is rapid, operationally simple, and chemoselective. The resulting aminooxy linker is stable under a variety of conditions and selectively cleavable in the presence of a low-oxidation-state transition metal. We have explored the full scope of this reaction using complex peptide systems and a recombinantly expressed protein.
