Solution and solid phase chemical synthesis of arabinonucleotides

1989 ◽  
Vol 67 (5) ◽  
pp. 831-839 ◽  
Author(s):  
Masad José Damha ◽  
Nassim Usman ◽  
Kelvin Kenneth Ogilvie
Keyword(s):  
Chemical Synthesis ◽  
Solid Phase ◽  
Building Blocks ◽  
Convenient Procedure ◽  
Phase Chemical

A fast and convenient procedure for the chemical synthesis of arabinonucleotides, which eliminates the multistep protection of the arabinonucleoside building blocks, is described. The results of these studies were successfully applied to the automated chemical synthesis of the hexanucleotide 5′-aUpaApaUpaApaUpaA-3′. Both solution and solid phase phosphite triester procedures are described. Keywords: arabinonucleotides, arabinophosphoramidites, automated chemical synthesis, protected arabinonucleosides.

Development of Strategies for Glycopeptide Synthesis: An Overview on the Glycosidic Linkage

2020 ◽  
Vol 24 (21) ◽  
pp. 2475-2497
Author(s):  
Andrea Verónica Rodríguez-Mayor ◽  
German Jesid Peralta-Camacho ◽  
Karen Johanna Cárdenas-Martínez ◽  
Javier Eduardo García-Castañeda
Keyword(s):  
Chemical Synthesis ◽  
Solid Phase ◽  
Building Blocks ◽  
Heterogeneous Environments ◽  
Phase Synthesis ◽  
Low Concentrations ◽  
Biological Sources ◽  
Synthetic Routes ◽  
The Impact ◽  
Potential Use

Glycoproteins and glycopeptides are an interesting focus of research, because of their potential use as therapeutic agents, since they are related to carbohydrate-carbohydrate, carbohydrate-protein, and carbohydrate-lipid interactions, which are commonly involved in biological processes. It has been established that natural glycoconjugates could be an important source of templates for the design and development of molecules with therapeutic applications. However, isolating large quantities of glycoconjugates from biological sources with the required purity is extremely complex, because these molecules are found in heterogeneous environments and in very low concentrations. As an alternative to solving this problem, the chemical synthesis of glycoconjugates has been developed. In this context, several methods for the synthesis of glycopeptides in solution and/or solid-phase have been reported. In most of these methods, glycosylated amino acid derivatives are used as building blocks for both solution and solid-phase synthesis. The synthetic viability of glycoconjugates is a critical parameter for allowing their use as drugs to mitigate the impact of microbial resistance and/or cancer. However, the chemical synthesis of glycoconjugates is a challenge, because these molecules possess multiple reaction sites and have a very specific stereochemistry. Therefore, it is necessary to design and implement synthetic routes, which may involve various protection schemes but can be stereoselective, environmentally friendly, and high-yielding. This review focuses on glycopeptide synthesis by recapitulating the progress made over the last 15 years.

Efficient Solid-Phase Chemical Synthesis of 5′-Triphosphates of DNA, RNA, and their Analogues

2010 ◽  
Vol 12 (10) ◽  
pp. 2190-2193 ◽  
Author(s):  
Ivan Zlatev ◽  
Thomas Lavergne ◽  
Françoise Debart ◽  
Jean-Jacques Vasseur ◽  
Muthiah Manoharan ◽  
...  
Keyword(s):  
Chemical Synthesis ◽  
Solid Phase ◽  
Phase Chemical

Fmoc-based solid phase chemical synthesis of 71-meric neuregulin 1-β1, an epidermal growth factor-like domain

2008 ◽  
Vol 14 (3) ◽  
pp. 261-266
Author(s):  
Taeko Kakizawa ◽  
Shizuyo Koide-Yoshida ◽  
Tooru Kimura ◽  
Hiromasa Uchimura ◽  
Yoshio Hayashi ◽  
...  
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Chemical Synthesis ◽  
Solid Phase ◽  
Neuregulin 1 ◽  
Epidermal Growth ◽  
Phase Chemical

Solid-Phase Chemical Synthesis of Phosphonoacetate and Thiophosphonoacetate Oligodeoxynucleotides

2003 ◽  
Vol 125 (4) ◽  
pp. 940-950 ◽  
Author(s):  
Douglas J. Dellinger ◽  
David M. Sheehan ◽  
Nanna K. Christensen ◽  
James G. Lindberg ◽  
Marvin H. Caruthers
Keyword(s):  
Chemical Synthesis ◽  
Solid Phase ◽  
Phase Chemical

Principles and Practice of Solid-Phase Peptide Synthesis

2002 ◽  
Author(s):  
Gregg B. Fields ◽  
Janelle L Lauer-Fields
Keyword(s):  
Amino Acid ◽  
Chemical Synthesis ◽  
Protease Inhibitors ◽  
Solid Phase ◽  
Building Blocks ◽  
Pharmaceutical Products ◽  
New Drugs ◽  
Side Chain ◽  
Amino Acid Residues ◽  
Functional Roles

Peptides play key structural and functional roles in biochemistry, pharmacology, and neurobiology, and are important probes for research in enzymology, immunology, and molecular biology. The amino acid building blocks can be among the 20 genetically encoded L-residues, or else unusual ones, and the sequences can be linear, cyclic, or branched. It follows that rapid, efficient, and reliable methodology for the chemical synthesis of these molecules is of utmost interest. A number of synthetic peptides are significant commercial or pharmaceutical products, ranging from the sweet dipeptide L-Asp-L-Phe-OMe (aspartame) to clinically used hormones such as oxytocin, adrenocorticotropic hormone, calcitonin, and gonadotropin releasing hormone (GnRH) super-agonists. Synthesis can lead to potent and selective new drugs by judicious substitutions that change functional groups and/or conformations of the parent peptide. These include introduction of N- or C-alkyl substituents, unnatural or D-amino acids, side-chain modifications including sulfate or phosphate groups or carbohydrate moieties, and constraints such as disulfide bridges between half-cystines or side-chain lactams between Lys and Asp or Glu. Commercially important products that evolved from such studies include protease inhibitors, such as captopril and other angiotensin converting enzyme (ACE) inhibitors, peptidomimetic HIV protease inhibitors, and the somatostatin analog lanreotide. Most of the biologically or medicinally important peptides which are the targets for useful structure-function studies by chemical synthesis comprise under 50 amino acid residues, but occasionally a synthetic approach can lead to important conclusions about small proteins (full or domains) in the 100-200 residue size range. Methods for synthesizing peptides are divided conveniently into two categories: solution (classical) and solid-phase pep tide synthesis (SPPS). The classical methods have evolved since the beginning of the twentieth century, and they are described amply in several reviews and books (Wünsch, 1974; Finn and Hofmann, 1976; Bodanszky and Bodanszky, 1984; Goodman et al, 2001). The solid-phase alternative was conceived and elaborated by R. B. Merrifield beginning in 1959, and has also been covered comprehensively (Erickson and Merrifield, 1976; Birr, 1978; Barany and Merrifield, 1979; Stewart and Young, 1984; Merrifield, 1986; Barany et al., 1987, 1988; Kent, 1988; Atherton and Sheppard, 1989; Fields and Noble, 1990; Barany and Albericio, 1991; Fields et al., 1992; Gutte, 1995; Fields, 1997; Lloyd-Williams et al., 1997; Chan and White, 2000; Kates and Albericio, 2000).

A NOVEL APPROACH TO SOLID PHASE CHEMICAL SYNTHESIS OF OLIGONUCLEOTIDE mRNA CAP ANALOGS

2005 ◽  
Vol 24 (5-7) ◽  
pp. 601-605 ◽  
Author(s):  
Jacek Jemielity ◽  
Petri Heinonen ◽  
Harri Lönnberg ◽  
Edward Darzynkiewicz
Keyword(s):  
Chemical Synthesis ◽  
Solid Phase ◽  
Novel Approach ◽  
Phase Chemical

scholarly journals Controlled Formation of Catalytic and Emissive Gold Nanoclusters with a Synthetic Self-Assembled Protein Toroid

2020 ◽  
Author(s):  
David Bouzada ◽  
Ester Polo ◽  
Elena López ◽  
Yolanda Pérez ◽  
Cristian Vidal ◽  
...  
Keyword(s):  
Chemical Synthesis ◽  
Self Assembly ◽  
Solid Phase ◽  
Recombinant Expression ◽  
Solid Phase Peptide Synthesis ◽  
Gold Nanoclusters ◽  
Building Blocks ◽  
Biophysical Characterization ◽  
Self Assembled

<div>Self-assembled proteins are privileged building blocks for the bottom-up organization of matter at the nanoscale. However, since most proteins are very large, they have to be produced by recombinant expression, which is less versatile and flexible than chemical synthesis. Here, we show that we can bridge the potential of proteins for nanofabrication with the simplicity and versatility of solid-phase peptide synthesis by relying on the self-assembly of the viral protein gp23.1, a small 50-residue protein that oligomerizes in solution to form a stable toroidal hexamer. We report the chemical synthesis and basic biophysical characterization of a gp23.1 mutant and show that its self-assembled hexamer templates the formation of highly monodisperse gold nanoclusters of about 1.3 nm inside its central cavity. The resulting nanoclusters show catalytic activity in cycloisomerization reactions as well as luminescence emission. This work demonstrates the versatility of this small self- assembled ring protein for a variety of nanotechnological applications.</div>

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