Evidence map›Paper›PMID 40322874›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2025

Late-Stage Amination of Peptides on the Solid Phase.

Julian Brinkhofer, Marius Werner, Agon Kokollari, Shih-Yu Pan, Christian Klein, Truc Lam Pham, Franziska Thomas

Abstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Article
  2. Late-Stage Functionalization of Peptides on the Solid Phase.Angewandte Chemie (International ed. in English) · 2026
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Julian BrinkhoferInstitute of Organic Chemistry, Heidelberg University, Im Neuenheimer Feld 270, 69120, Heidelberg, Germany.ORCID https://orcid.org/0009-0002-5722-6783
Marius WernerInstitute of Organic Chemistry, Heidelberg University, Im Neuenheimer Feld 270, 69120, Heidelberg, Germany.ORCID https://orcid.org/0000-0003-0926-2181
Agon KokollariInstitute of Organic Chemistry, Heidelberg University, Im Neuenheimer Feld 270, 69120, Heidelberg, Germany.ORCID https://orcid.org/0009-0007-9149-6644
Shih-Yu PanDepartment of Chemistry, Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo, 113-0033, Japan.ORCID https://orcid.org/0009-0005-8742-2656
Christian KleinInstitute of Pharmacy and Molecular Biotechnology (IPMB), Heidelberg University, Im Neuenheimer Feld 364, 69120, Heidelberg, Germany.ORCID https://orcid.org/0000-0003-3522-9182
Truc Lam PhamInstitute of Organic Chemistry, Heidelberg University, Im Neuenheimer Feld 270, 69120, Heidelberg, Germany.ORCID https://orcid.org/0000-0003-3808-2083
Franziska ThomasInstitute of Organic Chemistry, Heidelberg University, Im Neuenheimer Feld 270, 69120, Heidelberg, Germany.ORCID https://orcid.org/0000-0002-1176-7018

Funding

Bundesministerium für Bildung und Forschung ExU 6.1.16.3Deutsche Forschungsgemeinschaft 2082/1 390761711Max-Planck-Gesellschaft Matter to LifeMinisterium für Wissenschaft, Forschung und Kunst Baden-Württemberg ExU 6.1.16.3Verband der Chemischen Industrie Kekulé Fellowship
6 · The paper itself

Abstract

Late-stage peptide modification is a powerful tool for rapidly generating a library of peptide mimetics, for example, for drug discovery or catalyst development. While late-stage modifications exist for many types of structural features, methods for introducing amines into peptides via a late-stage approach are rare, despite their enormous potential for the development of peptide therapeutics. Here we present a protocol for introducing amines into peptides by our established on-resin iodination-substitution approach. Our method is compatible with a wide variety of amines, including primary and secondary amines, anilines, and other heteroaromatic N-nucleophiles mostly giving good to excellent yields. We introduce amines that are pharmacologically relevant as well as those that can impart catalytic or metal-binding properties into the peptide of interest. As a proof-of-concept study, we introduce the metal ligand tris(2-aminoethyl)amine (tren) into a tryptophan zipper scaffold using our late-stage amination approach to explore metal-induced stapling. Indeed, metal complexation via the tren ligand resulted in a thermal stabilization of more than 30 K in one of our tryptophan zipper designs.

Indexed as

AminesPeptidesAminationCatalysisLigandsSolid-Phase Synthesis TechniquesTryptophanAminesLigandsPeptidesTryptophanamineslate‐stage functionalizationpeptidessolid‐phase synthesistryptophan zippers

Identifiers

PMID40322874
PMCPMC12172594

What Socratic holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.