Part No: Issued year: 2013File size: 0.35mbFile type: pdf
Leu-Enkephalin-amide (YGGFLNH2, Ca. MW = 554.65) was synthesized on the Rink amide ChemMatrix® resin at a scale of 0.5 mmol. Crude peptide (100 mg) was purified in duplicate using the Isolera Dalton equipped with a Biotage® SNAP KP-C18-HS 12g cartridge.
Part No: AN097Issued year: 2014File size: 0.73mbFile type: pdf
A branched peptidoglycan mimic and a tetra-branched antimicrobial peptide analogue were synthesized on a lysine scaffold using Biotage® Initiator+ Alstra™ microwave peptide synthesizer. These peptide modifications are challenging to synthesize and automate, however, the procedure was operationally simplified using Branches™.
Part No: AN053Issued year: 2010File size: 0.92mbFile type: pdf
It has recently been demonstrated that specific recognition of rhizobial bacteria by the signaling molecule Nod-factor receptor 5 (NFR5) relies on LysM domains. The LysM (lysine motif) domain is believed to be involved in the regulation of the interaction between plants and rhizobial bacteria to promote plant growth. The LysM domain is predicted to consist of two-α
helices and a two-stranded anti-parallel β-sheet in a β-α-α-β structure and has been identified in NFR5 by sequence alignment of the crystal structure with the LysM domain of Bacillus subtilis ykuD.2 The synthesis of the C-terminal and the N-terminal regions of LysM domains provide significant challenges, this is presumably due to the formation of β-sheet like structures, which are known to pose problems for peptide chain assembly.
Part No: AN055Issued year: 2012File size: 0.28mbFile type: pdf
C-terminal peptide aldehydes are key components in oxime and hydrazine ligations and their synthesis is therefore very desirable. A well established method for the synthesis of C-terminal modified peptides including peptide aldehydes, is the backbone amide linker (BAL) strategy (Scheme 1).1 In this strategy, the first amino acid is anchored by reductive amination followed by acylation of the newly formed secondary amine. Thus, the growing peptide chain is anchored not through the C-terminal carboxyl but through a backbone amide nitrogen giving access to, in principle, any C-terminal modification.
Part No: AN054Issued year: 2011File size: 0.39mbFile type: pdf
A number of biologically active natural products contain N-methyl amino acids. N-Methyl amino acid containing peptides are potentially useful therapeutics as they have improved pharmacological properties such as such as proteolytic stability, bioavailability, lipophilicity, enhanced potency and receptor selectivity. The synthetic challenges associated with the synthesis of peptides containing consecutive N-methyl amino acids are well known1,2 and often require coupling reagents such as PyBOP3, HATU4 or even triphosgene4 to obtain high coupling yields. Syro Wave.
Part No: AN052Issued year: 2010File size: 0.26mbFile type: pdf
One of the current challenges in peptide science is the assembly of long peptides and small proteins, which has to overcome the accumulation of side-reactions and the hurdles posed by so-called difficult sequences. During the synthesis of difficult sequences the peptide chain most likely becomes partially inaccessible typically due to the formation of secondary structures, especially β-sheets, which can inhibit acylation and deprotection during synthesis, resulting in truncated sequences. In addition, steric hindrance from β-branched amino acids can be a problem.
Part No: Issued year: 2014File size: 1.01mbFile type: pdf
We have demonstrated the capability of the Biotage® Initiator+ Alstra
microwave peptide synthesizer to fully synthesize branched and cyclic
peptides. The synthesis included specialized reactions of non-linear peptides and a high degree of purity was achieved. Furthermore, the Branches software feature provides an extensive overview for the scheduling and visualization of operations in order to make complex peptide modifications and is a great addition to the toolbox for the peptide chemist. Presented at EPS, Sofia, 2014.
Part No: Issued year: 2005File size: 0.29mbFile type: pdf
Microwave technology at ChemDiv
Standard procedure for Suzuki coupling:
Building block 1-25 (0.25 mmol), the correspondent boronic acid (0.50 mmol) was heated under microwave irradiation (180oC, 10-40 min) in the presence of catalyst [PdCl2(PPh3)2 or dichlorobis(triphenyl-phosphine)palladium(II) polymer bound and Cs2CO3 as a base in DME/Water (50/50) as solvent.
Part No: AN081Issued year: 2014File size: 0.79mbFile type: pdf
This application demonstrates the reproducible multiple peptide
synthesis on a Syro parallel peptide synthesizer equipped with Syro
heating blocks. Effective heat transfer combined with efficient vortex
mixing make this system a powerful tool for the synthesis of multiple
peptides with increased throughput capability.
Part No: AN069Issued year: 2013File size: 0.47mbFile type: pdf
The human β-amyloid (1-42), H-DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA-NH2 (1), sequence is a wellknown difficult sequence to synthesize.1,2 This is due to its
high hydrophobicity at the C-terminus and on-resin aggregation. The peptide is known to be one of the main constituents in amyloid plaques in the brain of Alzheimer’s patients.
Synthetic amyloid peptides are essential research tools to study the molecular mechanisms of neurodegenerative diseases, however, their solid-phase assembly is non-trivial.
Part No: TN/UG-0029.0110Issued year: 2009File size: 0.75mbFile type: pdf
The Biotage Syro Wave™ system is a programmable peptide synthesizer that is capable of both conventional room temperature parallel peptide synthesis and microwave assisted peptide synthesis. The system is a fully automated and computer controlled peptide
synthesizer, based on a pipetting robot with a single arm.
Part No: Issued year: 2011File size: 0.23mbFile type: pdf
• Biologically active peptides isolated from natural sources, e.g. marine sponges, often contain multiple N-methylated residues. Additionally, Nmethylation of synthetic peptides can improve pharmacokinetic properties like bio-availability and stability.
Part No: TV-SS-02Issued year: 2010File size: 0.1mbFile type: pdf
The TurboVap II sensor is designed to monitor the concentration process. It does this with light and logic. The sample tube stem sits in a light beam at about 0.8mL for 1mL tubes and at 0.5mL for the 0.5mL tubes. Every second, a microprocessor receives an indication of the change in optical density of the solution being concentrated. Small changes in optical density over a thirty second period are registered to memory and become the new initial or zero point for the sensor to look at the next change. When the sample is done and the meniscus crosses the sensor beam, a large change in optical density takes place and the TurboVap II beeps. The change for either dark or clear must persist for several seconds for the sensor to beep. At this point the gas flow stops and an alarm sounds to indicate that the sample is complete. When the attendant looks at the control panel, a blinking light indicates which position is complete.