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Antibiotic ornament clasp

Lugdunin, a cyclic peptide with strong antimicrobial properties, works by proton transport across bacterial membranes. The researchers discovered that the thiazolidine group in lugdunin forms a critical part of its structure and is essential for its antibacterial activity.

SourceWiley·JournalAngewandte Chemie International Edition·DateMay 27, 2019

Fleming's method in miniature

Researchers at ETH Zurich develop a new technique, nanoFleming, to rapidly test for antibiotic activity in microorganisms. The method has identified 11 novel peptides with improved efficacy or resistance-bypassing properties.

SourceETH Zurich·JournalNature Chemical Biology·DateApr 29, 2019

About TFE: Old and new findings

Researchers review TFE's role as a structuring agent for unfolded peptides, inducing helical conformations, while also enhancing protein denaturation. The study details recent applications of TFE in conformational studies, including antimicrobial and aggregation-prone peptides.

SourceBentham Science Publishers·JournalCurrent Protein and Peptide Science·DateApr 4, 2019

Major step towards individual cancer immunotherapy

Scientists create vaccine that strengthens immune defences by multiplying cancer-repelling T cells, promising treatment for individualized cancer immunotherapy and potential application in autoimmune diseases. Laboratory tests conducted on tumours in mice show effectiveness of approach.

SourceETH Zurich·JournalNature Immunology·DateMar 29, 2019

How proteins become embedded in a cell membrane

A team of ETH Zurich researchers used single-molecule force spectroscopy to investigate how membrane proteins become embedded in cell membranes. They discovered the role of two helper proteins, insertase and translocase, which enable membrane proteins to embed themselves in the membrane. The study sheds light on the folding pathways of...

SourceETH Zurich·JournalScience Advances·DateFeb 14, 2019

Peptide papers point to new ways of tackling bacteria

Researchers have solved a 20-year riddle of how crucial step in antibiotic biosynthesis occurs, opening way to potentially redesigning antibiotics. The team structurally characterised the peptide bond forming domain in Ebony enzyme, revealing its novel types of condensation domain and its role in regulating neurotransmitters.

SourceMonash University·JournalProceedings of the National Academy of Sciences·DateJan 28, 2019

Using machine learning to design peptides

A new algorithm that combines experimental data with machine learning reduces the time needed to find optimal peptide sequences, allowing for faster discovery and synthesis. This method has the potential to revolutionize how peptides are designed and could lead to breakthroughs in materials science, chemistry, and medicine.

SourceNorthwestern University·JournalNature Communications·DateDec 10, 2018

Towards a treatment for gluten intolerance

A new study has identified a specific peptide that directly binds to the ion-channel CFTR, impairing its function and triggering cellular stress and inflammation. This interaction can be inhibited by a potentiator of CFTR, which may offer protection against gluten-induced intestinal symptoms.

SourceEMBO·JournalThe EMBO Journal·DateNov 30, 2018

Mutations boost immunity: Toward a cancer vaccine

Researchers develop method to identify tumor-specific factors in blood that can elicit a protective immune response, potentially leading to an effective vaccine against cancer. The technique relies on peptide arrays and frameshift mutations, which have been shown to be more effective stimulators of immune response than point mutations.

SourceArizona State University·JournalScientific Reports·DateNov 26, 2018

How do peptides penetrate cells? Two sides of the same coin

Scientists at IOCB Prague have discovered a previously unknown passive mechanism by which positively charged short peptides can penetrate cells. This process is based on membrane fusion induced by the transported peptides and shares the same mechanistic basis as known processes in neurons during nerve impulses.

En route to custom-designed natural products

Scientists have successfully explained the structure and function of docking domains in peptide natural products. This breakthrough allows researchers to redesign docking domain interactions, modulating the product spectrum of a rhabdopeptide-synthesizing NRPS. The discovery has promising implications for creating new substances.

SourceGoethe University Frankfurt·JournalNature Communications·DateOct 19, 2018

Ants surrender their venomous secrets

Researchers analyzed ant venom from a tropical species and identified over 2,800 venom peptides, including 37 full-length peptide precursors called myrmicitoxins. The peptides showed sequence similarities with those produced by other insects, suggesting they evolved from ancestral genes.

SourceAmerican Chemical Society·JournalJournal of Proteome Research·DateSep 12, 2018

Alzheimer's disease and type 2 diabetes: Hope for inhibitors against amyloid plaques

Scientists at TUM have discovered a new class of designed macrocyclic peptides that are highly potent inhibitors of amyloid formation, which could be an alternative to current antibody-based approaches. The researchers are now planning further investigations to verify their effectiveness in in vivo models.

SourceTechnical University of Munich (TUM)·JournalAngewandte Chemie International Edition·DateAug 7, 2018

UBC researchers create matchmaking service

Researchers at the University of British Columbia have created a matchmaking service to pair peptides with antibiotics, increasing treatment success rates against antimicrobial resistant bacteria. Seven combinations were identified that worked better than antibiotics alone, offering up to a 100-fold improvement.

SourceUniversity of British Columbia·JournalPLOS Pathogens·DateJun 21, 2018