A fusion protein combining a signal, stalk, and anchor domain positions the target molecule away from the cell membrane to resolve steric hindrance.
Genetically encoded unnatural amino acid initiators enable site-specific polymer growth from recombinant proteins via atom transfer radical polymerization.
Segmented domains enable a cyclic peptide to form continuous networks that overcome toxic synthetic matrices while preventing biofilm accumulation.
Segmenting the mature TAFA-4 region eliminates complex ligation steps, reducing manufacturing costs while maintaining therapeutic activity.
NIP-V peptide disrupts N protein dimerization to inhibit viral replication, addressing the lack of effective small-molecule treatments.
Brush polymers incorporate therapeutic peptides as side chains to resist proteolytic digestion and improve cellular uptake.
Dynamic peptide probes overcome solubility and stability limits by switching conformations upon binding, improving detection reliability.
Fluorinated acetamide reporters overcome steric hindrance in bulky chemical labels by enabling efficient global profiling of molecular targets.
KDM2B-mediated epigenetic reprogramming accelerates neural differentiation, reducing treatment time and improving recovery rates for injured spinal nerves.
A split intein construct excises itself from splice products to enable high-throughput detection of specific gene events.
Transglutaminase mediates site-specific conjugation of growth factors to fibronectin, eliminating non-selective by-products and complex purification steps.
Hydrophilic linker systems transform solid phase peptide synthesis into a homogeneous liquid phase process, reducing solvent waste and improving product purity.
Single-chain Alphabody libraries enable high-affinity binder selection through defined sequence variation in helix surface and linker regions.
Peptide administration resolves chronic wound stagnation by triggering intracellular signaling cascades that drive re-epithelialization and angiogenesis.
A dipeptide comprising a non-proteogenic amino acid enables efficient coupling with polypeptides using phosphonium reagents in aqueous media.