130622-08-1Relevant articles and documents
A concise synthesis of (S)-(-)-3-(2-carboxy-4-pyrrolyl)-alanine
Adamczyk, Maciej,Johnson, Donald D.,Reddy, Rajarathnam E.
, p. 3063 - 3068 (2000)
A convergent synthesis of (S)-(-)-3-(2-carboxy-4-pyrrolyl)-alanine (CPA) 1, a non-proteinogenic amino acid is described starting from a commercially available dimethyl L-aspartate 2 in good overall yield. Copyright (C) 2000 Elsevier Science Ltd.
A facile synthesis of (S)-gizzerosine, a potent agonist of the histamine H2-receptor
Fanning, Kate N.,Sutherland, Andrew
, p. 8479 - 8481 (2007)
A simple and direct approach for the synthesis of (S)-gizzerosine, an amino acid responsible for the disease, black vomit, and a potent histamine H2-receptor, has been developed in 10 steps and in 31% overall yield from l-aspartic acid. The key steps involved a two-carbon homologation of an l-aspartic acid semi-aldehyde and direct alkylation of unprotected histamine with a 6-hydroxynorleucine derivative.
A short and efficient synthesis of (S)-(+)-2-(Hydroxymethyl)-6-piperidin-2- one
Upadhyay, Puspesh K.,Kumar, Pradeep
, p. 2512 - 2514 (2010)
A concise synthesis of (S)-(+)-2-(hydroxymethyl)-6-piperidin-2-one is described that employs l-aspartic acid as chiral pool starting material and Wittig reaction as the key step. Georg Thieme Verlag Stuttgart - New York.
Substrate Engineering in Lipase-Catalyzed Selective Polymerization of d -/ l -Aspartates and Diols to Prepare Helical Chiral Polyester
Zhang, Yu,Xia, Bo,Li, Yanyan,Lin, Xianfu,Wu, Qi
, p. 918 - 926 (2021)
The synthesis of optically pure polymers is one of the most challenging tasks in polymer chemistry. Herein, Novozym 435 (Lipase B from Candida antarctica, immobilized on Lewatit VP OC 1600)-catalyzed polycondensation between d-/l-aspartic acid (Asp) diester and diols for the preparation of helical chiral polyesters was reported. Compared with d-Asp diesters, the fast-reacting l-Asp diesters easily reacted with diols to provide a series of chiral polyesters containing N-substitutional l-Asp repeating units. Besides amino acid configuration, N-substituent side chains and the chain length of diols were also investigated and optimized. It was found that bulky acyl N-substitutional groups like N-Boc and N-Cbz were more favorable for this polymerization than small ones probably due to competitively binding of these small acyl groups into the active site of Novozym 435. The highest molecular weight can reach up to 39.5 × 103 g/mol (Mw, D = 1.64). Moreover, the slow-reacting d-Asp diesters were also successfully polymerized by modifying the substrate structure to create a "nonchiral"condensation environment artificially. These enantiocomplementary chiral polyesters are thermally stable and have specific helical structures, which was confirmed by circular dichroism (CD) spectra, scanning electron microscope (SEM), and molecular calculation.
Synthesis of Imidazole and Histidine-Derived Cross-Linkers as Analogues of GOLD and Desmosine
Sch?del, Nicole,Icik, Esra,Martini, Maike,Altevogt, Luca,Ramming, Isabell,Greulich, Andreas,Baro, Angelika,Bilitewski, Ursula,Laschat, Sabine
supporting information, p. 2260 - 2268 (2021/03/04)
Amino acid derivatives with a central cationic heterocyclic core (e.g., imidazolium) are biologically relevant cross-linkers of proteins and advanced glycation end (AGE) products. Here, imidazolium-containing cross-linkers were synthesized from imidazole or histidine by N-alkylation employing aspartate- and glutamate-derived mesylates as key step. Biological investigations were carried out to probe the biocompatibility of these compounds.
Selenolysine: A New Tool for Traceless Isopeptide Bond Formation
Dardashti, Rebecca Notis,Kumar, Shailesh,Sternisha, Shawn M.,Reddy, Post Sai,Miller, Brian G.,Metanis, Norman
supporting information, p. 4952 - 4957 (2020/04/07)
Despite their biological importance, post-translationally modified proteins are notoriously difficult to produce in a homogeneous fashion by using conventional expression systems. Chemical protein synthesis or semisynthesis offers a solution to this problem; however, traditional strategies often rely on sulfur-based chemistry that is incompatible with the presence of any cysteine residues in the target protein. To overcome these limitations, we present the design and synthesis of γ-selenolysine, a selenol-containing form of the commonly modified proteinogenic amino acid, lysine. The utility of γ-selenolysine is demonstrated with the traceless ligation of the small ubiquitin-like modifier protein, SUMO-1, to a peptide segment of human glucokinase. The resulting polypeptide is poised for native chemical ligation and chemoselective deselenization in the presence of unprotected cysteine residues. Selenolysine's straightforward synthesis and incorporation into synthetic peptides marks it as a universal handle for conjugating any ubiquitin-like modifying protein to its target.