Browse
Submit Data
Databases
API
Help

Dataset Information

21 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Design, synthesis, and photochemical validation of peptide linchpins containing the S,S-tetrazine phototrigger.

ABSTRACT: The design, solid-phase synthesis, and photochemical validation of diverse peptide linchpins, containing the S,S-tetrazine phototrigger, have been achieved. Steady state irradiation or femtosecond laser pulses confirm their rapid photofragmentation. Attachment of peptides to the C- and N-termini will provide access to diverse constrained peptide constructs that hold the promise of providing information about early peptide/protein conformational dynamics upon photochemical release.

SUBMITTER: Abdo M

PROVIDER: S-EPMC3397404 | biostudies-literature | 2012 Jul

REPOSITORIES: biostudies-literature

ACCESS DATA

Json Xml

Publications

Design, synthesis, and photochemical validation of peptide linchpins containing the S,S-tetrazine phototrigger.

Abdo Mohannad M Brown Stephen P SP Courter Joel R JR Tucker Matthew J MJ Hochstrasser Robin M RM Smith Amos B AB

Organic letters 20120626 13

The design, solid-phase synthesis, and photochemical validation of diverse peptide linchpins, containing the S,S-tetrazine phototrigger, have been achieved. Steady state irradiation or femtosecond laser pulses confirm their rapid photofragmentation. Attachment of peptides to the C- and N-termini will provide access to diverse constrained peptide constructs that hold the promise of providing information about early peptide/protein conformational dynamics upon photochemical release. ...[more]

PMID: 22731895

Similar Datasets

Peptide/protein stapling and unstapling: introduction of s-tetrazine, photochemical release, and regeneration of the peptide/protein.

Project description:Protocols have been achieved that permit facile introduction of s-tetrazine into unprotected peptides and the protein, thioredoxin, between two cysteine sulfhydryl groups (i.e., staple), followed by photochemical release (i.e., unstaple) and regeneration of the peptide/protein upon removal of the cyano groups from the derived bisthiocyanate. The S,S-tetrazine macrocycles in turn provide a convenient handle for probe introduction by exploiting the inverse electron demand Diels-Alder reactivity of the tetrazine.

| S-EPMC4394111 | biostudies-literature

The design and synthesis of alanine-rich ?-helical peptides constrained by an S,S-tetrazine photochemical trigger: a fragment union approach.

Project description:The design and synthesis of alanine-rich ?-helical peptides constrained in a partially unfolded state by incorporation of the S,S-tetrazine phototrigger has been achieved, permitting, upon photochemical release, observation by 2D-IR spectroscopy of the subnanosecond conformational dynamics that govern the early steps associated with ?-helix formation. Solid-phase peptide synthesis was employed to elaborate the requisite fragments, with full peptide construction via solution-phase fragment condensation. The fragment union tactic was also employed to construct (13)C?(18)O isotopically edited amides to permit direct observation of conformational motion at or near specific peptide bonds.

| S-EPMC3916828 | biostudies-other

Tetrazine-Containing Amino Acid for Peptide Modification and Live Cell Labeling.

Project description:A novel amino acid derivative 3-(4-(1, 2, 4, 5-tetrazine-3-yl) phenyl)-2-aminopropanoic acid was synthesized in this study. The compound possessed better water-solubility and was synthesized more easily compared with the well-known and commercially available 3-(p-benzylamino)-1, 2, 4, 5-tetrazine. Tetrazine-containing amino acid showed excellent stability in biological media and might be used for cancer cell labeling. Moreover, the compound remained relatively stable in 50% TFA/DCM with little decomposition after prolonged exposure at room temperature. The compound could be utilized as phenylalanine or tyrosine analogue in peptide modification, and the tetrazine-containing peptide demonstrated more significant biological activity than that of the parent peptide. The combination of tetrazine group and amino acid offered broad development prospects of the bioorthogonal labeling and peptide synthesis.

| S-EPMC4633098 | biostudies-literature

In situ synthesis of peptide microarrays - shadow mask design

Project description:This SuperSeries is composed of the SubSeries listed below. Refer to individual Series

2014-01-16 | E-GEOD-50045 | biostudies-arrayexpress

In situ synthesis of peptide microarrays - shadow mask design

Project description:This SuperSeries is composed of the SubSeries listed below.

2014-01-16 | GSE50045 | GEO

In situ synthesis of peptide microarrays - shadow mask design [1]

Project description:A computer program was used to create random amino acid sequences based on and restricted by physical shadow masks which will be used for lithography-based synthesis of peptides. The output from this algorithm was used to create peptides that were synthesized by Sigma Aldrich, and printed onto glass slides. The arrays contained 384 peptides printed in duplicate for each of 4 different mask designs. 52 different monoclonal antibodies were incubated on these microarrays and analyzed for their propensity to bind the peptides created from each mask set. The diversity of binding served as a proxy for the 'randomness' of these peptides, and provided information about how many masks are needed to truly generate random sequence peptides. two replicates of each peptide was printed on 1 Mask peptide microarray. A minimum of Two microarrays were tested for each sample. Image was qualified using in-house metrics for quality assurance.

2014-01-16 | E-GEOD-49217 | biostudies-arrayexpress

In situ synthesis of peptide microarrays - shadow mask design [3]

Project description:In this paper several computer programs were used to simulate in situ synthesis of peptides using shadow masks and BOC synthesis. The peptides were designed to be random, or pseudo-random, but fulfill requirements of immunosignaturing. This file contains data from actual 330,000 peptide arrays that used the first iteration of the peptide generation algorithm. Monoclonal antibodies were bound to the microarrays and the total number of peptides that distinguished each monoclonal was measured. This provides a baseline against which to compare purely random sequences. One replicate of each peptide was printed on 1 330k peptide microarray. One microarray were tested for each sample. Image was qualified using in-house metrics for quality assurance.

2014-01-16 | E-GEOD-50571 | biostudies-arrayexpress

In situ synthesis of peptide microarrays - shadow mask design [2]

Project description:An experiment was designed to use a computer program to create lithography masks using a pseudo-random pattern generator. The data in this file are results from immunosignaturing 8 different monoclonals using a 10,000 peptide random-sequence microarray. Peptides were synthesized by Sigma Aldrich, and printed onto glass slides and used to test several different parameters. One replicate of each peptide was printed on 1 CIM_10K_v2 peptide microarray. One microarray were tested for each sample. Image was qualified using in-house metrics for quality assurance.

2014-01-16 | E-GEOD-50044 | biostudies-arrayexpress

In situ synthesis of peptide microarrays - shadow mask design [2]

2014-01-16 | GSE50044 | GEO

In situ synthesis of peptide microarrays - shadow mask design [1]

2014-01-16 | GSE49217 | GEO