Light-controllable dithienylethene-modified cyclic peptides: photoswitching the in vivo toxicity in zebrafish embryos

• Sergii Afonin,
• Oleg Babii,
• Aline Reuter,
• Volker Middel,
• Masanari Takamiya,
• Uwe Strähle,
• Igor V. Komarov and
• Anne S. Ulrich

Beilstein J. Org. Chem. 2020, 16, 39–49, doi:10.3762/bjoc.16.6

• peptide synthesis technology [3][4] have enabled peptide production at industrial scales, the exploration of therapeutic peptides as potential drugs is rapidly developing [4][5][6]. It has been shown that peptide drugs are less immunogenic than biologics and can hit the “undruggable” space of molecular

• , especially for preclinical drug candidate screenings. However, to the best of our knowledge, such applications for therapeutic peptides are still sparse [41][42][43][44][45]. Notably, zebrafish embryos are transparent, which makes them ideal for in vivo manipulation of photosensitive compounds [46]. This has

Peptide synthesis: ball-milling, in solution, or on solid support, what is the best strategy?

• Ophélie Maurin,
• Pascal Verdié,
• Gilles Subra,
• Frédéric Lamaty,
• Jean Martinez and
• Thomas-Xavier Métro

Beilstein J. Org. Chem. 2017, 13, 2087–2093, doi:10.3762/bjoc.13.206

• to improve their in vivo bioavailability and stability. This progresses empowered the potential of therapeutic peptides, suggesting a production surge in the future. Besides this high potential, actual peptide production techniques suffer from major environmental issues [4][5][6]. Indeed, large

Synthesis of constrained analogues of tryptophan

• Elisabetta Rossi,
• Valentina Pirovano,
• Marco Negrato,
• Giorgio Abbiati and
• Monica Dell’Acqua

Beilstein J. Org. Chem. 2015, 11, 1997–2006, doi:10.3762/bjoc.11.216

• hormone (GnRH) [13][14], Figure 2 (C). Finally, in the field of therapeutic peptides, constrained tryptophan residues of the β-carboline family (L-Tpi and D-Tpi), were used by Grieco and co-workers in the study and development of urotensin-II receptor (UTR) peptide ligands [15], Figure 2 (D). Switching

Automated solid-phase peptide synthesis to obtain therapeutic peptides

• Veronika Mäde,
• Sylvia Els-Heindl and
• Annette G. Beck-Sickinger

Beilstein J. Org. Chem. 2014, 10, 1197–1212, doi:10.3762/bjoc.10.118

• : automated synthesis; automation; lipidation; PEGylation; peptide drugs; solid-phase peptide synthesis; therapeutic peptides; Introduction Peptides and proteins are involved in a large variety of biochemical processes and physiological functions. Peptides can consist of up to 50 amino acids and have

• significantly smaller in size and hence, easier and cheaper to synthesize using chemical strategies [5]. Thereby, they provide a vast perspective for novel drug design. Table 1 summarizes valuable virtues and pivotal shortcomings of therapeutic peptides compared to traditional small organic molecules. The high

• more predictable in vivo behavior owed to their biochemical nature [7]. The extended size and the tremendous biological and chemical diversity of peptides opposed to small organic drugs opens targets for multiple applications [10]. In the last decades, the production of therapeutic peptides has been