Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

A general strategy for the preparation of C-terminal peptide alpha-ketoacids by solid phase peptide synthesis.

ABSTRACT: A new cyanosulfur-ylide based linker makes possible the synthesis of C-terminal peptide alpha-ketoacids by solid phase synthesis. The preparation of the requisite linker and its application to a variety of C-terminal peptide alpha-ketoacids with unprotected side chains is reported.

SUBMITTER: Ju L

PROVIDER: S-EPMC2907649 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature

ACCESS DATA

Json Xml

Publications

A general strategy for the preparation of C-terminal peptide alpha-ketoacids by solid phase peptide synthesis.

Ju Lei L Bode Jeffrey W JW

Organic & biomolecular chemistry 20090402 11

A new cyanosulfur-ylide based linker makes possible the synthesis of C-terminal peptide alpha-ketoacids by solid phase synthesis. The preparation of the requisite linker and its application to a variety of C-terminal peptide alpha-ketoacids with unprotected side chains is reported. ...[more]

PMID: 19462032

Similar Datasets

Preparation and Application of an Inexpensive α-Formylglycine Building Block Compatible with Fmoc Solid-Phase Peptide Synthesis.

Project description:α-Formylglycine (fGly) is a rare residue located in the active site of sulfatases and serves as a precursor to pharmaceutically relevant motifs. The installation of fGly motifs into peptides is currently challenging due to degradation under the acidic and nucleophile-rich conditions accompanying resin cleavage during solid-phase peptide synthesis. We report the synthesis of acid- and nucleophile-tolerant α-formylglycine building blocks from vitamin C and use them to prepare callyaerin A, a macrocyclic peptide containing an fGly-derived motif.

| S-EPMC10071478 | biostudies-literature

Preparation and Use of a General Solid-Phase Intermediate to Biomimetic Scaffolds and Peptide Condensations.

Project description:The Distributed Drug Discovery (D3) program develops simple, powerful, and reproducible procedures to enable the distributed synthesis of large numbers of potential drugs for neglected diseases. The synthetic protocols are solid-phase based and inspired by published work. One promising article reported that many biomimetic molecules based on diverse scaffolds with three or more sites of variable substitution can be synthesized in one or two steps from a common key aldehyde intermediate. This intermediate was prepared by the ozonolysis of a precursor functionalized at two variable sites, restricting their presence in the subsequently formed scaffolds to ozone compatible functional groups. To broaden the scope of the groups available at one of these variable sites, we developed a synthetic route to an alternative, orthogonally protected key intermediate that allows the incorporation of ozone sensitive groups after the ozonolysis step. The utility of this orthogonally protected intermediate is demonstrated in the synthesis of several representative biomimetic scaffolds containing ozonolytically labile functional groups. It is compatible with traditional Fmoc peptide chemistry, permitting it to incorporate peptide fragments for use in fragment condensations with peptides containing cysteine at the N-terminus. Overall yields for its synthesis and utilization (as many as 13 steps) indicate good conversions at each step.

| S-EPMC6100553 | biostudies-literature

An alpha-formylglycine building block for fmoc-based solid-phase peptide synthesis.

Project description:[reaction: see text] Nearly all known sulfatases share a common active site modification that is required for their activity: conversion of cysteine to alpha-formylglycine. We report the synthesis of an alpha-formylglycine building block suitable for Fmoc-based solid-phase peptide synthesis. The building block was incorporated into a synthetic peptide derived from the active site of a Mycobacterium tuberculosis sulfatase.

| S-EPMC2527029 | biostudies-literature

Solid-phase peptide synthesis and solid-phase fragment coupling mediated by isonitriles.

Project description:The synthesis of polypeptides on solid phase via mediation by isonitriles is described. The acyl donor is a thioacid, which presumably reacts with the isonitrile to generate a thio-formimidate carboxylate mixed anhydride intermediate. Applications of this chemistry to reiterative solid-phase peptide synthesis as well as solid-phase fragment coupling are described.

| S-EPMC3718127 | biostudies-literature

A reagent for the convenient, solid-phase synthesis of N-terminal peptide hydroxylamines for chemoselective ligations.

Project description:A new N-sulfonyloxaziridine reagent for the conversion of N-terminal peptide amines to the corresponding hydroxylamines without overoxidation or erosion of stereochemistry is described. The products are N-terminal hydroxylamines, which are substrates for chemoselective amide-bond forming reactions with alpha-ketoacids. The success of this reagent arises from covalent precomplexation with the substrate via imine bond formation followed by an intramolecular oxygen-atom transfer to the amine. An unexpected stereochemical mismatch between the racemic reagent and the chiral peptide substrates was addressed by the preparation of an enantipure version of this reagent and provides further support for the proposed mechanism.

| S-EPMC2677186 | biostudies-literature

Solid-phase synthesis of C-terminal peptide libraries for studying the specificity of enzymatic protein prenylation.

Project description:Prenylation is an essential post-translational modification in all eukaryotes. Here we describe the synthesis of a 340-member library of peptides containing free C-termini on cellulose membranes. The resulting library was then used to probe the specificity of protein farnesyltransferase from S. cerevisiae.

| S-EPMC3682486 | biostudies-literature

Recyclable hypervalent-iodine-mediated solid-phase peptide synthesis and cyclic peptide synthesis.

Project description:The system of the hypervalent iodine(III) reagent FPID and (4-MeOC6H4)3P was successfully applied to solid-phase peptide synthesis and cyclic peptide synthesis. Four peptides with biological activities were synthesized through SPPS and the bioactive cyclic heptapeptide pseudostellarin D was obtained via solution-phase peptide synthesis. It is worth noting that FPID can be readily regenerated after the peptide coupling reaction.

| S-EPMC6009197 | biostudies-literature

Total wash elimination for solid phase peptide synthesis.

Project description:We present a process for solid phase peptide synthesis (SPPS) that completely eliminates all solvent intensive washing steps during each amino acid addition cycle. A key breakthrough is the removal of a volatile Fmoc deprotection base through bulk evaporation at elevated temperature while preventing condensation on the vessel surfaces with a directed headspace gas flushing. This process was demonstrated at both research and production scales without any impact on product quality and when applied to a variety of challenging sequences (up to 89 amino acids in length). The overall result is an extremely fast, high purity, scalable process with a massive waste reduction (up to 95%) while only requiring 10-15% of the standard amount of base used. This transformation of SPPS represents a step-change in peptide manufacturing process efficiency, and should encourage expanded access to peptide-based therapeutics.

| S-EPMC10710472 | biostudies-literature

Solid Phase Peptide Synthesis on Chitosan Thin Films.

Project description:Stable chitosan thin films can be promising substrates for creating nanometric peptide-bound polyglucosamine layers. Those are of scientific interest since they can have certain structural similarities to bacterial peptidoglycans. Such films were deposited by spin coating from chitosan solutions and modified by acetylation and N-protected amino acids. The masses of deposited materials and their stability in aqueous solutions at different pH values and water interaction were determined with a quartz crystal microbalance with dissipation (QCM-D). The evolution of the surface composition was followed by X-ray photoelectron (XPS) and attenuated total reflectance infrared (ATR-IR) spectroscopy. Morphological changes were measured by atomic force microscopy (AFM), while the surface wettability was monitored by by static water contact angle measurements. The combination of the characterization techniques enabled an insight into the surface chemistry for each treatment step and confirmed the acetylation and coupling of N-protected glycine peptides. The developed procedures are seen as first steps toward preparing thin layers of acetylated chitin, potentially imitating the nanometric peptide substituted glycan layers found in bacterial cell walls.

| S-EPMC8924862 | biostudies-literature

Preparation of Enzyme-Activated Thapsigargin Prodrugs by Solid-Phase Synthesis.

Project description:Since cells in solid tumors divide less rapidly than cells in the bone marrow or cells of the immune system, mitotic inhibitors often cause severe side effects when used for treatment of diseases like prostate cancer and breast cancer. One approach to overcome this problem involves attempts at developing drugs based on general cytotoxins, like calicheamicin and thapsigargin, which kill cells at all phases of the cell cycle. However, such toxins can only be used when efficient targeting to the malignant tissue is possible. In the case of thapsigargin, selectivity for tumor-associated cells is achieved by conjugating the drug to a peptide that is only cleaved in the vicinity of tumors to release the cytotoxic drug or an analog with retained activity. Solid-phase synthesis protocols were developed for preparation of three already validated prodrugs of thapsigargin: one prodrug cleavable by human kallikrein 2, one prodrug cleavable by prostate-specific antigen, and one prodrug cleavable by prostate-specific membrane antigen.

| S-EPMC6100299 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data