Converting disulfide bridges in native peptides to stable methylene thioacetals

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Metal ions are indispensable cofactors for many proteins and play crucial roles in numerous biological processes, yet the computational design of metalloproteins and the optimization of metal coordination sites poses significant challenges due to the comp ...

In recent years, there has been a surge of interest in predicting computed activation barriers, to enable the acceleration of the automated exploration of reaction networks. Consequently, various predictive approaches have emerged, ranging from graph-based ...

Macrocycles provide an attractive modality for drug development but the identification of ligands to targets of interest is hindered by the lack of large macrocyclic compound libraries for high-throughput screening. A strategy to efficiently synthesize lar ...

Tris-(2-carboxyethyl)phosphine (TCEP) linked to agarose beads is widely used for reducing disulfide bridges in proteins and peptides. The immobilization of TCEP on beads allows efficient removal after reduction to prevent its reaction with alkylating reage ...

Macrocycles have raised much interest in the pharmaceutical industry due to their ability to bind challenging targets while often still being able to cross membranes to reach intracellular proteins. However, the development of macrocyclic ligands to new di ...

Thiol groups are suitable handles for site-selectively modifying, immobilizing or cyclizing individual peptides or entire peptide libraries. A limiting step in producing the thiol-functionalized peptides is the chromatographic purification, which is partic ...

The synthesis of large numbers of cyclic peptides-required, for example, in screens for drug development-is currently limited by the need of chromatographic purification of individual peptides. Herein, we have developed a strategy in which cyclic peptides ...

Macrocycles are an attractive class of molecules due to their good binding properties and yet rather small size that allows, in many cases, crossing membranes to reach intracellular targets. In comparison to classical small molecule drugs, macrocycles are ...

Computational protein design has emerged as a powerful tool capable of identifying sequences compatible with pre-defined protein structures. The sequence design protocols, implemented in the Rosetta suite, have become widely used in the protein engineering ...

Life is a non-equilibrium phenomenon. Owing to their high free energy content, the macromolecules of life tend to spontaneously react with ambient oxygen and water and turn into more stable inorganic molecules. A similar thermodynamic picture applies to th ...

Selective functionalization of peptides and proteins has always been a valuable tool for the study and manipulation of biological processes. In this context, cysteines are of particular interest. Their intrinsic high nucleophilicity makes these amino acids ...

DNA-encoded chemical library technologies enable the screening of large combinatorial libraries of chemically and structurally diverse molecules, including short cyclic peptides. A challenge in the combinatorial synthesis of cyclic peptides is the final st ...

Mutational analysis is widely used to study the relationship between sequence and structure of proteins and peptides. It is often assumed that substituting a proline with another amino acid "locks" the peptide bond in the trans conformation, allowing only ...

Biomolecular functional complexes often serve as inspiration for the development of artificial molecular nanostructures. The functionality of the biomolecular structures is based on complex and adaptable binding motifs that have evolved over billions of ye ...

The exquisite structural and optical characteristics of single-walled carbon nanotubes (SWCNTs), combined with the tunable specificities of proteins and peptides, can be exploited to strongly benefit technologies with applications in fields ranging from bi ...

Cyclic peptide therapeutics fill the gap between small molecules (5000 Da) as a separate class of drugs, combining the advantages of both in terms of high selectivity, bioavailability, synthetic accessibility and low toxicity. Howe ...

Mass spectrometry (MS) has emerged over the last two decades as the analytical technique of choice in systems-level protein studies, known as proteomics. Two are the MS-based approaches generally applied to proteomics: bottom-up (BU), which relies on the p ...

The disulfide bonds that form between two cysteine residues are important in defining and rigidifying the structures of proteins and peptides. In polypeptides containing multiple cysteine residues, disulfide isomerization can lead to multiple products with ...

Tandem mass spectrometry (MS/MS) combined with collision-induced dissociation (CID) is a key method for primary structure determination of peptides and proteins. Collisionally activated peptides undergo statistical dissociation, forming a series of backbon ...

Conformationally constrained peptide ligands offer an attractive format for the development of therapeutics. They can bind with high affinity and selectivity to protein targets, they are small enough to diffuse into tissues, they can be synthesized chemica ...

Converting disulfide bridges in native peptides to stable methylene thioacetals

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Engineering of stable and functional metalloproteins using evolutionary computation, deep learning and simulation

Benchmarking machine-readable vectors of chemical reactions on computed activation barriers

Methods for high-throughput synthesis and screening of peptide libraries

High-Density Immobilization of TCEP on Silica Beads for Efficient Disulfide Reduction and Thiol Alkylation in Peptides

Development of methods for the synthesis of large combinatorial libraries of macrocyclic compounds

Solid-phase peptide synthesis on disulfide-linker resin followed by reductive release affords pure thiol-functionalized peptides

Cyclative Release Strategy to Obtain Pure Cyclic Peptides Directly from the Solid Phase

Methods for the generation of large combinatorial macrocycle libraries

A Rosetta-based protein design protocol converging to natural sequences

Repair or Degrade: the Thermodynamic Dilemma of Cellular Protein Quality-Control

Application of Hypervalent Iodine Reagents for Novel Cysteine Labeling

Synthesis of DNA‐encoded disulfide‐ and thioether‐cyclized peptides

Can Mutational Analysis Be Used To Assist Structure Determination of Peptides?

Molecular Imaging of Biopolymers Enabled by Electrospray-Ion Beam Deposition

Noncovalent Protein and Peptide Functionalization of Single-Walled Carbon Nanotubes for Biodelivery and Optical Sensing Applications

Development of Stapling Methods by Selective Side Chain Modifications of Bioactive Peptides

Middle-down approaches for mass spectrometry-based protein identification and characterization

Dithiol amino acids can structurally shape and enhance the ligand-binding properties of polypeptides

Spectroscopic studies of peptide fragments produced by collision-induced dissociation

Development of bicyclic peptide Her2 binders and phage selection of alpha-helical peptide ligands