Entry to 2-aminoprolines via electrochemical decarboxylative amidation of N‑acetylamino malonic acid monoesters

• Olesja Koleda,
• Janis Sadauskis,
• Darja Antonenko,
• Edvards Janis Treijs,
• Raivis Davis Steberis and
• Edgars Suna

Beilstein J. Org. Chem. 2025, 21, 630–638, doi:10.3762/bjoc.21.50

• under constant current conditions in aqueous acetonitrile and provides access to N-sulfonyl, N-benzoyl, and N-Boc-protected 2-aminoproline derivatives. Keywords: anodic oxidation; decarboxylation; electrosynthesis; Hofer–Moest reaction; non-proteinogenic amino acids; Introduction Non-proteinogenic

Methyltransferases from RiPP pathways: shaping the landscape of natural product chemistry

• Maria-Paula Schröder,
• Isabel P.-M. Pfeiffer and
• Silja Mordhorst

Beilstein J. Org. Chem. 2024, 20, 1652–1670, doi:10.3762/bjoc.20.147

• contrast to ribosomal peptide biosynthesis, many non-proteinogenic amino acids can be incorporated as building blocks. However, RiPP pathways are more flexible and they represent interesting biotechnological production routes. In this review, we will focus on post-translational methylation reactions. A

• . However, using SAM supply or regeneration systems may be useful if the peptide substrate cannot be synthesised ribosomally, e.g., if it contains non-proteinogenic amino acids that cannot be produced by post-translational modifications of RiPP pathways. SAM supply or SAM regeneration systems typically

Discovery of unguisin J, a new cyclic peptide from Aspergillus heteromorphus CBS 117.55, and phylogeny-based bioinformatic analysis of UngA NRPS domains

• Sharmila Neupane,
• Marcelo Rodrigues de Amorim and
• Elizabeth Skellam

Beilstein J. Org. Chem. 2024, 20, 321–330, doi:10.3762/bjoc.20.32

• positions 1 (ᴅ-Ala) and 7 (GABA) are conserved but there is considerable variability at positions 2–6, including the incorporation of additional non-proteinogenic amino acids β-methylphenylalanine (βMePhe) and kynurenine (Kyn) [3][4]. So far, no significant biological activities have been reported for these

Reductive opening of a cyclopropane ring in the Ni(II) coordination environment: a route to functionalized dehydroalanine and cysteine derivatives

• Oleg A. Levitskiy,
• Olga I. Aglamazova,
• Yuri K. Grishin and
• Tatiana V. Magdesieva

Beilstein J. Org. Chem. 2022, 18, 1166–1176, doi:10.3762/bjoc.18.121

• -activity and chirality provided by the Ni–Schiff base template, supported with the protection from redox-destruction of the amino acid skeleton, makes the suggested approach a convenient route to various types of non-proteinogenic amino acids [9][10][12][13]. Recently, several practical approaches to α,α

N-Acylated amino acid methyl esters from marine Roseobacter group bacteria

• Hilke Bruns,
• Lisa Ziesche,
• Nargis Khakin Taniwal,
• Laura Wolter,
• Thorsten Brinkhoff,
• Jennifer Herrmann,
• Rolf Müller and
• Stefan Schulz

Beilstein J. Org. Chem. 2018, 14, 2964–2973, doi:10.3762/bjoc.14.276

• might indicate some similarity to homoserine in AHLs because both are non-proteinogenic amino acids. This similarity might also be functional, because the structures of NAMEs, NABMEs, NAGMEs and NAVMEs are similar to other bacterial signalling compounds, often carrying a lipophilic side chain and a

Iodination of carbohydrate-derived 1,2-oxazines to enantiopure 5-iodo-3,6-dihydro-2H-1,2-oxazines and subsequent palladium-catalyzed cross-coupling reactions

• Michal Medvecký,
• Igor Linder,
• Luise Schefzig,
• Hans-Ulrich Reissig and
• Reinhold Zimmer

Beilstein J. Org. Chem. 2016, 12, 2898–2905, doi:10.3762/bjoc.12.289

• [36] in Heck reactions [37][38][39][40][41][42] is also of interest, since these coupling products are useful intermediates for the synthesis of non-proteinogenic amino acids [43]. To our delight, the Heck coupling of syn-4a and 16 could be efficiently achieved employing Jeffery´s conditions [44

Muraymycin nucleoside-peptide antibiotics: uridine-derived natural products as lead structures for the development of novel antibacterial agents

• Daniel Wiegmann,
• Stefan Koppermann,
• Marius Wirth,
• Giuliana Niro,
• Kristin Leyerer and
• Christian Ducho

Beilstein J. Org. Chem. 2016, 12, 769–795, doi:10.3762/bjoc.12.77

• synthetase (NRPS) system appears to be responsible for the assembly of the urea tripeptide building block 105. However, the non-proteinogenic amino acids need to be formed first. It has been proposed that L-arginine (106) undergoes 3-hydroxylation (giving 3-hydroxy-L-arginine (107)) and subsequent ring

Natural products from microbes associated with insects

• Christine Beemelmanns,
• Huijuan Guo,
• Maja Rischer and
• Michael Poulsen

Beilstein J. Org. Chem. 2016, 12, 314–327, doi:10.3762/bjoc.12.34

• cultures of M. anisopliae, a commercial biocontrol product called Green Muscle [129]. Serinocyclin A contains several non-proteinogenic amino acids. Among them are the uncommon 1-aminocyclopropane-1-carboxylic acid, (2R,4S)-4-hydroxylysine, and the more frequently encountered hydroxyproline, β-alanine, and

Recent highlights in biosynthesis research using stable isotopes

• Jan Rinkel and
• Jeroen S. Dickschat

Beilstein J. Org. Chem. 2015, 11, 2493–2508, doi:10.3762/bjoc.11.271

• -ribosomal peptides Non-ribosomal peptides often exhibit a high bioactivity and are biosynthesized by non-ribosomal peptide synthethases (NRPS) [33], which work RNA-independent and catalyze the assembly of both proteinogenic and non-proteinogenic amino acids in a modular fashion. Moreover, NRPSs can contain

Synthesis of constrained analogues of tryptophan

• Elisabetta Rossi,
• Valentina Pirovano,
• Marco Negrato,
• Giorgio Abbiati and
• Monica Dell’Acqua

Beilstein J. Org. Chem. 2015, 11, 1997–2006, doi:10.3762/bjoc.11.216

• naturally occurring or chemically synthesized non-proteinogenic amino acids are classified [1]. Chemically synthesized non-proteinogenic amino acids embody in principle a countless collection of assorted chemical structures and are mainly employed as they are or as scaffolds for pharmacologically active

Automated solid-phase peptide synthesis to obtain therapeutic peptides

• Veronika Mäde,
• Sylvia Els-Heindl and
• Annette G. Beck-Sickinger

Beilstein J. Org. Chem. 2014, 10, 1197–1212, doi:10.3762/bjoc.10.118

• -proteinogenic amino acids such as D- [84] or N-methylated [85][86] monomers or general truncation or mutation of biologically not relevant positions creating peptide analogs [87]. Likewise, backbone manipulation by partial or complete cyclization [88] as well as incorporation of peptide bond mimetics [89] can

• the integration of peptides into particles, gels or liposomes [14][82][83]. Recently, the great methodical repertoire for extending the half-lifes of biological active peptides by covalent chemical approaches has been reviewed [8]. These methods include peptide sequence modifications by non

Peptides presenting the binding site of human CD4 for the HIV-1 envelope glycoprotein gp120

• Julia Meier,
• Kristin Kassler,
• Heinrich Sticht and
• Jutta Eichler

Beilstein J. Org. Chem. 2012, 8, 1858–1866, doi:10.3762/bjoc.8.214

• -proteinogenic amino acids, and the modification of the peptide backbone. Such modifications widen the chemical and structural diversity exhibited by peptides, as well as improve their proteolytic stability, increasing their prospects for pharmaceutical use. Therefore, peptides are excellent candidates as

• underlying the protein function. Furthermore, such mimetic molecules are promising candidates for the inhibition of protein–protein interactions. Synthetic peptides can be produced as direct reproductions of protein fragments and by diverse chemical modification, including the integration of non