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

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.

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Fmoc Solid Phase Peptide Synthesis

10.1093/oso/9780199637256.001.0001 ◽

1999 ◽

Cited By ~ 19

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.

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Pyrrole-Mediated Peptide Cyclization Identified through Genetically Reprogrammed Peptide Synthesis

Biomedicines ◽

10.3390/biomedicines6040099 ◽

2018 ◽

Vol 6 (4) ◽

pp. 99 ◽

Cited By ~ 2

Author(s):

Klaas Decoene ◽

Willem Vannecke ◽

Toby Passioura ◽

Hiroaki Suga ◽

Annemieke Madder

Keyword(s):

Peptide Synthesis ◽

Cyclic Peptide ◽

Solid Phase ◽

Solid Phase Peptide Synthesis ◽

Screening Method ◽

In Vitro Translation ◽

Side Chain ◽

One Pot ◽

Depth Analysis

Flexible in vitro translation (FIT) was used as a screening method to uncover a new methodology for peptide constraining based on the attack of a nucleophilic side-chain functionality onto an oxidized furylalanine side chain. A set of template peptides, each containing furylalanine as furan-modified amino acid and a nucleophilic residue (Cys, His, Lys, Arg, Ser, or Tyr), was produced through FIT. The translation mixtures were treated with N-bromosuccinimide (NBS) to achieve selective furan oxidation and subsequent MALDI analysis demonstrated Lys and Ser as promising residues for cyclisation. Solid-phase peptide synthesis (SPPS) was used to synthesize suitable amounts of material for further in-depth analysis and characterisation. It was found that in the case of the peptide containing lysine next to a furylalanine residue, a one-pot oxidation and reduction reaction leads to the generation of a cyclic peptide featuring a pyrrole moiety as cyclisation motif, resulting from the attack of the lysine side chain onto the oxidized furylalanine side chain. Structural evidence was provided via NMR and the generality of the methodology was explored. We hereby expand the scope of our previously developed furan-based peptide labeling and crosslinking strategy.

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

10.1101/2020.05.21.109215 ◽

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.

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