Dipl.-Chem. Robert Zitterbart

Profil

Zusammenfassung

Robert Zitterbart entwickelt Methoden zur chemischen Synthese und Reinigung von Peptiden und Proteinen ohne klassische HPLC, mit Fokus auf Parallelisierbarkeit und Nachhaltigkeit. Seine Expertise umfasst die Festphasensynthese, native chemische Ligationen und innovative Aufreinigungstechniken, die es ermöglichen, mehrere Peptide gleichzeitig zu verarbeiten und dabei Kosten sowie Umweltbelastung zu senken.

Skills

Name

Dipl.-Chem. Robert Zitterbart

Titel

Dipl.-Chem.

Fakultät

Mathematisch-Naturwissenschaftliche Fakultät

Institut

Institut für Chemie

Arbeitsgruppe

Organische und Bioorganische Chemie III

E-Mail

🔒 nur für eingeloggte sichtbarAnmelden

Telefon

🔒 nur für eingeloggte sichtbarAnmelden

HU-FIS-Profil

Quelle ↗

Zuletzt gescrapt

28.6.2026, 01:15:08

• Skalierbare, parallele & nachhaltige HPLC-freie Reinigung von Peptiden durch eine chemische Affinitätschromatographie

  Quelle ↗

  Förderer: Bundesministerium für Wirtschaft und Energie Zeitraum: 09/2016 - 04/2018 Projektleitung: Dipl.-Chem. Robert Zitterbart, Prof. Dr. rer. nat. Oliver Seitz

🔒 Das System hat 113 mögliche Industrie-Partner gefunden — Firmen, Scores und Begründungen sind nur für eingeloggte Nutzer:innen sichtbar. Anmelden

• Total chemical synthesis of proteins without HPLC purification

  2016

  Chemical Science · 62 Zitationen · DOI

  the hydrolysed peptide thioester (which does not contain a C-terminal peptide hydrazide). Finally, the target protein is released with diluted hydrazine or acid. We applied the method in the synthesis of 46 to 126 amino acid long MUC1 proteins comprising 2-6 copies of a 20mer tandem repeat sequence. Only three days were required for the parallel synthesis of 9 MUC1 proteins which were obtained in 8-33% overall yield with 90-98% purity despite the omission of HPLC purification.

• Parallel Chemical Protein Synthesis on a Surface Enables the Rapid Analysis of the Phosphoregulation of SH3 Domains

  2016

  Angewandte Chemie International Edition · 28 Zitationen · DOI

  Analysis of postranslationally modified protein domains is complicated by an availability problem, as recombinant methods rarely allow site-specificity at will. Although total synthesis enables full control over posttranslational and other modifications, chemical approaches are limited to shorter peptides. To solve this problem, we herein describe a method that combines a) immobilization of N-terminally thiolated peptide hydrazides by hydrazone ligation, b) on-surface native chemical ligation with self-purified peptide thioesters, c) radical-induced desulfurization, and d) a surface-based fluorescence binding assay for functional characterization. We used the method to rapidly investigate 20 SH3 domains, with a focus on their phosphoregulation. The analysis suggests that tyrosine phosphorylation of SH3 domains found in Abl kinases act as a switch that can induce both the loss and, unexpectedly, gain of affinity for proline-rich ligands.

• Optimization of peptide synthesis time and sustainability using novel eco‐friendly binary solvent systems with induction heating on an automated peptide synthesizer

  2024

  Journal of Peptide Science · 23 Zitationen · DOI

  On December 12th, 2023, the European Commission took regulatory action to amend Annex XVII of REACH, imposing restrictions on the use of N,N-dimethylformamide (DMF) within the EU market owing to its high toxicity. Historically, DMF has been widely considered the gold standard for solid-phase peptide synthesis (SPPS). Being urgent to propose alternative solvents, we tested the suitability of non-hazardous neat and mixed solvents. Notably, binary solvent mixtures containing dimethyl sulfoxide as one of the solvent partners demonstrated high efficacy in solubilizing reagents while maintaining the desired swelling characteristics of common resins. A series of binary solvent mixtures were tested in automated SPPS, both at room temperature and high temperature, employing the PurePep® Chorus synthesizer, which enabled controlled induction heating between 25 and 90°C with oscillation mixing. The performances were assessed in challenging peptide sequences, i.e., ACP (65-74), and in longer and aggregating sequences like SARS-CoV-2 RBM (436-507) and β-amyloid (1-42). Furthermore, as part of the proposed sustainable approach to minimize the utilization of hazardous solvents, we coupled the novel PurePep EasyClean catch-and-release purification technology. This work, addressing regulatory compliance, emphasizes the crucial role of green chemistry in advancing safer and more environmentally friendly practices in SPPS.

Aus HU-FIS sind keine Kooperationen für diese Person gemeldet.