Rapid On-Resin N-Formylation of Peptides as One-Pot Reaction [Research Data] (doi:10.11588/data/00RULE)

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Document Description

Citation

Title:

Rapid On-Resin N-Formylation of Peptides as One-Pot Reaction [Research Data]

Identification Number:

doi:10.11588/data/00RULE

Distributor:

heiDATA

Date of Distribution:

2024-02-09

Version:

1

Bibliographic Citation:

Kokollari, Agon; Werner, Marius; Lindner, Christina; Pham, Truc Lam; Thomas, Franziska, 2024, "Rapid On-Resin N-Formylation of Peptides as One-Pot Reaction [Research Data]", https://doi.org/10.11588/data/00RULE, heiDATA, V1

Study Description

Citation

Title:

Rapid On-Resin N-Formylation of Peptides as One-Pot Reaction [Research Data]

Identification Number:

doi:10.11588/data/00RULE

Authoring Entity:

Kokollari, Agon (Heidelberg University)

Werner, Marius (Heidelberg University)

Lindner, Christina (Heidelberg University)

Pham, Truc Lam (Heidelberg University)

Thomas, Franziska (Heidelberg University)

Grant Number:

414261058, 2082/1–390761711 (3DMM2O)

Grant Number:

Kekulé Fellowship (T.L.P)

Distributor:

heiDATA

Access Authority:

Thomas, Franziska

Access Authority:

Pham, Truc Lam

Date of Deposit:

2024-01-31

Holdings Information:

https://doi.org/10.11588/data/00RULE

Study Scope

Keywords:

Chemistry, chemotactic peptides, late-stage formylation, post-translational modification, protein modifications, solid-phase synthesis

Abstract:

N-formylation is a common pre- and post-translational modification of the N-terminus or the lysine side chain of peptides and proteins that plays a role in the initiation of immune responses, gene expression, or epigenetics. Despite its high biological relevance, protocols for the chemical N-formylation of synthetic peptides are scarce. The few available methods are elaborate in their execution and the yields are highly sequence-dependent. We present a rapid, easy-to-use one-pot procedure that runs at room temperature and can be used to formylate protected peptides at both the N-terminus and the lysine side chain on the resin in near-quantitative yields. Only insensitive, storage-stable standard chemicals – formic acid, acetic anhydride, pyridine and DMF – are used. Formylation works for both short and long peptides of up to 34 amino acids and over the spectrum of canonical amino acids.

Methodology and Processing

Sources Statement

Data Access

Other Study Description Materials

Related Publications

Citation

Title:

A. Kokollari, M. Werner, C. Lindner, T. L. Pham, F. Thomas, ChemBioChem 2023, e202300571.

Identification Number:

10.1002/cbic.202300571

Bibliographic Citation:

A. Kokollari, M. Werner, C. Lindner, T. L. Pham, F. Thomas, ChemBioChem 2023, e202300571.

Other Study-Related Materials

Label:

1_Optimization_of_P1_formylation.zip

Notes:

application/zip

Other Study-Related Materials

Label:

2_Formylation_of_P2_to_P6.zip

Notes:

application/zip

Other Study-Related Materials

Label:

Original_Data_Overview.docx

Notes:

application/vnd.openxmlformats-officedocument.wordprocessingml.document

Other Study-Related Materials

Label:

Original_Data_Overview.pdf

Notes:

application/pdf