scholarly journals Design and Validation of a Frugal, Automated, Solid-Phase Peptide Synthesizer

2020 ◽  
Author(s):  
Nathaniel E. Kallmyer ◽  
Nathan E. Rider ◽  
Nigel F. Reuel
Keyword(s):  
Peptide Synthesis ◽  
Self Assembly ◽  
Synthetic Peptides ◽  
Materials Science ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Fluid Handling ◽  
Price Point ◽  
Grade Fluid ◽  
Chemistry Laboratories

AbstractSolid phase peptide synthesis (SPPS) has enabled widespread use of synthetic peptides in applications ranging from pharmaceuticals to materials science. The demand for synthetic peptides has driven recent efforts to produce automated SPPS synthesizers which utilize fluid-handling components common to chemistry laboratories to drive costs down to several thousand dollars. Herein, we describe the design and validation of a more ‘frugal’ SPPS synthesizer that uses inexpensive, consumer-grade fluid-handling components to achieve a prototype price point between US$300 and $600. We demonstrated functionality by preparing and characterizing peptides with a variety of distinct properties including binding functionality, nanoscale self-assembly, and oxidation-induced fluorescence. This system yielded micromoles of peptide at a cost of approximately $1/residue, a cost which may be further reduced by optimization and bulk purchasing.

scholarly journals Synthetic peptides caged on histidine residues with a bisbipyridyl ruthenium(ii) complex that can be photolyzed by visible light

2015 ◽  
Vol 51 (25) ◽  
pp. 5501-5504 ◽  
Author(s):  
Jesús Mosquera ◽  
Mateo I. Sánchez ◽  
José L. Mascareñas ◽  
M. Eugenio Vázquez
Keyword(s):  
Visible Light ◽  
Peptide Synthesis ◽  
Building Block ◽  
Synthetic Peptides ◽  
Solid Phase ◽  
Ruthenium Complex ◽  
Solid Phase Peptide Synthesis ◽  
Side Chain ◽  
Histidine Residues

We report a light-sensitive histidine building block for Fmoc/tBu solid-phase peptide synthesis in which the imidazole side chain is coordinated to a ruthenium complex.

scholarly journals Efficient Synthesis of Peptides with 4-Methylpiperidine as Fmoc Removal Reagent by Solid Phase Synthesis

2017 ◽  
Vol 58 (4) ◽  
Author(s):  
Javier Eduardo García Castañeda ◽  
Cristian Francisco Vergel Galeano ◽  
Zuly Jenny Rivera Monroy ◽  
Javier Eduardo Rosas Pérez
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Peptide Synthesis ◽  
Synthetic Peptides ◽  
Solid Phase Synthesis ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Amino Group ◽  
Efficient Synthesis ◽  
Phase Synthesis

<p>Solid phase peptide synthesis using the Fmoc/<em>t</em>-Bu strategy (SPPS-Fmoc/tBu) is the most widely used methodology for obtaining synthetic peptides. In this paper, we evaluate the viability of using 4-methylpiperidine as a reagent for deprotection of the amino acid alpha amino group in SPPS-Fmoc/tBu. For this purpose, the peptide (RRWQWRMKKLG) was simultaneously synthesized using 4-methylpiperidine or piperidine for Fmoc removal reagent. The obtained products had similar purities and yields. Finally, 21 peptides were synthesized using 4-methylpiperidine. Our results suggest that is possible to obtain synthetic peptides efficiently by the strategy SPPS-Fmoc/tBu when 4-methylpiperidine was used as reagent to remove Fmoc groups N-alpha protected amino acids.</p>

A Strategy for Thioamide Incorporation During Fmoc Solid-Phase Peptide Synthesis with Robust Stereochemical Integrity

2019 ◽  
Author(s):  
luis camacho III ◽  
Bryan J. Lampkin ◽  
Brett VanVeller
Keyword(s):  
Amino Acid ◽  
Functional Groups ◽  
Peptide Synthesis ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Side Chains ◽  
Amino Acid Side Chains ◽  
Peptide Elongation

We describe a method to protect the sensitive stereochemistry of the thioamide—in analogy to the protection of the functional groups of amino acid side chains—in order to preserve the thioamide moiety during peptide elongation.<br>

Analytical Methods for Solid Phase Peptide Synthesis

2004 ◽  
Vol 8 (4) ◽  
pp. 291-301 ◽  
Author(s):  
Giuseppina Sabatino ◽  
Mario Chelli ◽  
Alberto Brandi ◽  
Anna Papini
Keyword(s):  
Peptide Synthesis ◽  
Analytical Methods ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis

Fmoc Solid Phase Peptide Synthesis

1999 ◽  
Keyword(s):  
Peptide Synthesis ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Peptide Chain ◽  
Standard Approach ◽  
Side Chain ◽  
Complex Structures ◽  
Protein Conjugation ◽  
Chemoselective Ligation ◽  
Routine Production

In the years since the publication of Atherton and Sheppard's volume, the technique of Fmoc solid-phase peptide synthesis has matured considerably and is now the standard approach for the routine production of peptides. The basic problems outstanding at the time of publication of this earlier work have now been, for the most part, solved. As a result, innovators in the field have focussed their efforts to develop methodologies and chemistry for the synthesis of more complex structures. The focus of this new volume is much broader, and covers not only the essential procedures for the production of linear peptides but also more advanced techniques for preparing cyclic, side-chain modified, phospho- and glycopeptides. Many other methods also deserving attention have been included: convergent peptide synthesis; peptide-protein conjugation; chemoselective ligation; and chemoselective purification. The difficult preparation of cysteine and methionine-containing peptides is also covered, as well as methods for overcoming aggregation during peptide chain assembly and a survey of available automated instrumentation.

scholarly journals Cover Picture: Propylphosphonic Anhydride (T3P®) as Coupling Reagent for Solid‐Phase Peptide Synthesis (11/2021)

2021 ◽  
Vol 6 (11) ◽  
pp. 2648-2648
Author(s):  
Othman Al Musaimi ◽  
Richard Wisdom ◽  
Peter Talbiersky ◽  
Beatriz G. De La Torre ◽  
Fernando Albericio
Keyword(s):  
Peptide Synthesis ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Coupling Reagent
Sign in / Sign up

Export Citation Format

Share Document