Peptide Publications Archive
Locking Peptide Shape
Spring and Yudin Labs
Macrocyclic peptides fold into multiple conformations, frustrating efforts to fix their three-dimensional shape. A new rhodium-catalyzed strategy now builds a biaryl "dominant rotor" directly into …
Lasso Peptide Surgery
Chu Lab
Lasso peptides are mechanically interlocked natural products whose knotted topology has made them resistant to chemical editing. A new chemoenzymatic strategy cuts and re-seals the …
Lattice by Sequence
Weil Lab
Peptide self-assembly has long relied on lengthy sequences or external scaffolds to achieve ordered porous architectures. Now, researchers show that a nine-residue peptide alone can …
Assembling Retroaldolases
Korendovych Lab
Designing enzymes from scratch is hard; nature took billions of years to do it. A new study shows that short peptides can spontaneously self-assemble into …
Fluorinated Core Evolution
Suga Lab
Protein hydrophobic cores packed almost entirely with fluorinated amino acids were thought to be incompatible with defined biological function. A new selection platform challenged that …
Minimal CSP Scaffolds
Tal-Gan Lab
Quorum sensing in Streptococcus sinensis depends on a competence-stimulating peptide whose minimum functional requirements were completely unknown. Reverse alanine scanning now reveals that nearly one-third …
SuFEx Locks Rings
Fan and Mi Teams
Metal-free macrocyclization has long been a bottleneck for DNA-encoded peptide libraries. A new SuFEx-based strategy closes rings in aqueous buffer within minutes, scales to 343 …
Glycine Builds Collagen
Raines Lab
The collagen triple helix is nature's most abundant protein fold, yet chemists have long assumed it requires proline and hydroxyproline to form. New work shows …
Blue-Light Uncaging
Banghart Lab
One-photon photopharmacology in the brain has long depended on UV or violet light, with its poor tissue penetration and phototoxicity concerns. A new caged opioid …
Pairing for Scale
Heinis Lab
Chemical peptide libraries in microwell plates have rarely exceeded a few thousand members, leaving a vast chemical space unreachable by functional screening. A disulfide-pairing strategy …
Pocket Engineering Polymyxin
Kries Lab
Polymyxin antibiotics save lives but cause kidney damage and face rising resistance. A single amino acid substitution in a biosynthetic enzyme now enables direct fermentative …
Tryptophan Quenches All
Vendrell Lab
Fluorogenic amino acids that span the full visible spectrum could transform wash-free cell imaging and drug screening, but no single intramolecular quenching motif had proven …
Lysine Covalent Capture
Baker Group
Cysteine-targeting covalent warheads dominate drug design, yet cysteine is the rarest amino acid in proteins and nearly absent from protein-protein interfaces. A new lysine-reactive chemistry …
Atomic Edits, Altered Assemblies
Conticello Lab
Swapping a single atom in a self-assembling peptide sequence can reshape the entire supramolecular architecture, even when the resulting filaments look nearly identical under a …
Disulfide Architecture Decoded
Raj Lab
Disulfide bonds in peptides are typically treated as chemically identical, forcing chemists to reduce them all before making any modification. A new architecture-guided approach reveals …
Azapeptides on Autopilot
Proulx Lab
Aza-amino acid substitutions can lock bioactive conformations and resist proteases, but the chemistry that builds them has stubbornly resisted automation. A new protocol adapts every …
Unlocking Amanitin ADCs
Perrin Lab
α-Amanitin kills cancer cells regardless of proliferation status, making it an attractive antibody–drug conjugate payload. Yet its signature non-canonical amino acid, dihydroxyisoleucine, had never been …
Painting Amyloid
Rüdiger and Friedler labs
Amyloid fibrils in Alzheimer's and Huntington's disease desperately need better molecular tools, yet most peptide scaffolds offer little chemical flexibility. A new modular peptide family …
Timing the Tunnel
Terry Moore Lab
Type II proline-rich antimicrobial peptides kill bacteria by trapping release factors inside the ribosome, yet no biophysical method existed to measure how tightly they bind …
Sacrificial Shields
Raines Lab
Histidine drives catalysis in roughly one-fifth of all enzymes, yet oxidative damage to its imidazole ring is irreversible. A study of human ribonuclease 1 now …
Designing Molecular Switches
Baker Lab
Chemically induced dimerization systems give researchers on/off control over cellular processes, but existing tools borrow from nature and carry off-target liabilities. A new approach builds …
Tagging Nanobodies Precisely
Distefano Lab
Conventional nanobody conjugation generates heterogeneous products that erode imaging performance in vivo. A new chemoenzymatic strategy using farnesyltransferase installs two orthogonal bioorthogonal handles in a …
Lipophilic Cation Switch
Waters Lab
Peptidomimetic inhibitors of histone reader proteins carry a fundamental contradiction: the cationic residues required for tight binding actively sabotage cell entry. A new class of …
Silencing the Warhead
Derda Lab
Covalent genetically encoded peptide libraries hold enormous promise for discovering irreversible inhibitors, but installing reactive electrophilic warheads under basic conditions causes those warheads to quench …