Industrial Routes from Sugars and Biomass to CMF and Other 5-(Halomethyl)furfurals.

The synthesis of 5-(halomethyl)furfurals (XMFs, X=F, Cl, Br, I), including 5-(chloromethyl)furfural (CMF), 5-(bromomethyl)furfural (BMF), 5-(iodomethyl)furfural (IMF), and 5-(fluoromethyl)furfural (FMF), from biomass represents a pivotal advancement in renewable chemistry and engineering. Harnessing waste biomass as a raw material offers a sustainable alternative to fossil-based resources, mitigating environmental degradation and addressing pressing energy needs. CMF and BMF, characterized by their enhanced stability over the hydroxyl analog, 5-(hydroxymethyl)furfural (HMF), exhibit promise as renewable building blocks for scale-up and commercialization. The surge in research interest, particularly from 2010 to 2024, reflects a growing recognition of XMFs' potential as novel platform chemicals. This review highlights the evolution of XMF synthesis methods, focusing on their transformation from saccharides and lignocellulosic biomass. Mechanistic insights and experimental setups are scrutinized for industrial feasibility and scalability, shedding light on technical challenges and avenues for further research. The analysis underscores the burgeoning significance of XMFs in the transition towards sustainable chemical production, emphasizing the importance of process optimization and mechanistic understanding for commercial deployment.

Binding Dynamics of a Stapled Peptide Targeting the Transcription Factor NF-Y.

Transcription factors (TFs) play a central role in gene regulation, and their malfunction can result in a plethora of severe diseases. TFs are therefore interesting therapeutic targets, but their involvement in protein-protein interaction networks and the frequent lack of well-defined binding pockets render them challenging targets for classical small molecules. As an alternative, peptide-based scaffolds have proven useful, in particular with an α-helical active conformation. Peptide-based strategies often require extensive structural optimization efforts, which could benefit from a more detailed understanding of the dynamics in inhibitor/protein interactions. In this study, we investigate how truncated stapled α-helical peptides interact with the transcription factor Nuclear Factor-Y (NF-Y). We identified a 13-mer minimal binding core region, for which two crystal structures with an altered C-terminal peptide conformation when bound to NF-Y were obtained. Subsequent molecular dynamics simulations confirmed that the C-terminal part of the stapled peptide is indeed relatively flexible while still showing defined interactions with NF-Y. Our findings highlight the importance of flexibility in the bound state of peptides, which can contribute to overall binding affinity.