Research 🤝 Industry 🤝 Policy Science is all about collaboration. That’s why we at the Leibniz-HKI were so excited to welcome Bundestag member Sascha van Beek on his summer tour focused on Neglected T...

The European oil beetle's parasitic larvae emit a floral scent that attracts wild bees. This allows the larvae to sneak into the bees' nests

Nature Reviews Chemistry - Ahead of his 60th birthday, Guy Lloyd-Jones, Forbes Professor of Organic Chemistry at the University of Edinburgh, spoke about his career in science.

Heme, an iron-containing cofactor, is synthesized in mitochondria by an eight-enzyme pathway. Although cells were thought to manage heme autonomously, more than 1000 proteins contribute to its product...

Biological processes rely on finely tuned homo- and heteromeric interactions between (biomacro)molecules. The strength of an interaction, typically given by the dissociation constant (KD), plays a crucial role in basic research and must be monitored throughout the development of drugs and agrochemicals. An ideal method for KD determination is applicable to various analytes with a large range of affinities, tolerates complex matrix compositions, does not require labeling, and simultaneously provides information on the structural integrity of the binding partners. Native mass spectrometry meets these criteria but typically struggles with homooligomeric complexes due to overlapping mass signals. To overcome this, we resolve monomer/dimer contributions to overlapping MS-peaks by separately analyzing the charge state distribution of each oligomeric species via sample dilution and covalent cross-linking. Following this approach, we show that quantitative laser-induced liquid bead ion desorption mass spectrometry (qLILBID-MS) accurately captures the affinities of Bovine Serum Albumin (BSA) and chemically induced dimers of Tryparedoxin (Tpx), an oxidoreductase from human pathogenic Trypanosoma brucei parasites, with various molecular glues and homodimer affinities. Conveniently, qLILBID-MS requires a fraction of sample used by other methods such as isothermal titration calorimetry (ITC) and yields previously inaccessible protein homodimer KDs in the high micromolar range, which allowed us to monitor the gradual decrease in homodimer affinity via mutation of crucial dimer interface contacts. Overall, qLILBID-MS is a sensitive, robust, fast, scalable, and cost-effective alternative to quantify protein/protein interactions, that can accelerate contemporary drug discovery workflows, e.g. the efficient screening for proximity inducing molecules like proteolysis targeting chimera (PROTACs) and molecular glues.

European regulators greenlight new one-dose compound that could help African countries get rid of an ancient burden

The peptidases can break bonds between specific <small>D</small>- and <small>L</small>-amino acids, filling a gap in the toolbox for natural products characterization

Peptidases are indispensable tools in biotechnology and chemical biology. However, the enzyme repertoire for the selective hydrolysis of dl-amide bonds in peptides is small. Here, we describe novel dl-peptidases that mediate complex microbial interactions. These enzymes, Lip3 and Lip7, convert lipopeptides into potent amoebicidal agents via selective dl-peptide bond cleavage. Using structural analyses and mutagenesis, we identified an unusual Ser–Lys–Lys–Tyr catalytic tetrad required for dl-specificity. Despite their high structural similarity, both enzymes show distinct substrate preferences: Lip3 acts primarily as a carboxypeptidase, removing a single C-terminal residue, while Lip7 excises a tripeptide. Although their substrate scopes are broad, they are highly specific with regard to their respective cutting sites. These features make these dl-peptidases powerful tools for elucidating the structure of complex peptide-based natural products, including tensin and WLIP. Overall, this work elucidates the molecular mechanisms of cooperative microbial defense and provides a new enzymatic toolbox for biocatalysis and natural product discovery.

Peptidases are indispensable tools in biotechnology and chemical biology. However, the enzyme repertoire for the selective hydrolysis of dl-amide bonds in peptides is small. Here, we describe novel dl...

Seit 100 Jahren können Bakterien mit Antibiotika gut behandelt werden. Doch inzwischen sind auch multiresistente Keime im Umlauf, die immun gegen die Medikamente sind. An der Uni Jena forscht man an e...

Researchers in the Cluster of Excellence “Balance of the Microverse” at the University of Jena decipher a key mechanism of antibiotic resistance pumps

17th German Peptide Symposium, University of Duisburg-Essen, 04.-06.03.2026, Group Professor Markus Kaiser

The enzyme carbonic anhydrase mediates the taste sensation of carbonated drinks.

YouTube video by Universität Jena

Bacterially produced antimicrobial peptides (AMPs), or bacteriocins, play key roles in shaping microbial communities via interspecies competition. Unlike the more temporally dynamic gut microbiome, the oral microbiome exhibits long-term stability and is preserved into deep time in dental calculus, enabling evolutionary analysis across time. Here, we combine metagenomics, structural modeling, and experimental validation to investigate AMP diversity in ancient and modern dental biofilms from humans, Neanderthals, and nonhuman primates spanning 100,000 years. Using our newly developed platform, AMPcombi, we uncover evolutionary trajectories of bacteriocins and elucidate their ecological functions. Among these, we identify a conserved family of Actinomyces-derived defensin-like peptides, termed actifensins, present across all time periods. Phylogenetic, structural, and functional analyses revealed shared ancestry and adaptive diversification between ancient (paleo-) and modern actifensins, with evidence of positive selection and maintained antimicrobial activity. Our findings position the oral microbiome as a valuable reservoir for natural product discovery. In the face of rising antimicrobial resistance, evolutionary insights into AMP function open a door to next-generation therapeutics. AMPcombi streamlines this process, linking ancient biomolecules with biotechnology.

The ankyrin repeat is one of the most abundant protein-protein interaction motifs in eukaryotes yet occurs in only a small number of ion channels. These channels are all members of the transient recep...

The communication hinge, found in type IV ABC transporters, forms a bidirectional communication between ATP- and substrate-binding sites. This is an unexplored allosteric pathway critical for function...

Nature Communications - The communication hinge, found in type IV ABC transporters, forms a bidirectional communication between ATP- and substrate-binding sites. This is an unexplored allosteric...

Biological processes rely on finely tuned homo- and heteromeric interactions between (biomacro)molecules. The strength of an interaction, typically given by the dissociation constant (KD), plays a cru...

Sickle cell disease (SCD), an inherited blood disorder caused by a mutation in the &beta;-globin gene, is characterized by sickle erythrocytes that are ...