Surface-immobilized ampetoids resolve the cytotoxicity trade-off by combining active killing with passive antifouling barriers.
XTEN fusion proteins extend growth hormone serum half-life from minutes to days, reducing dosing frequency without increasing immunogenicity.
Anti-viral peptoids occupy the ACE2 receptor to block virus entry, preserving enzymatic activity while offering stable treatment options.
Positive-Helix-Hydrophobic Peptides enable efficient transmembrane delivery while reducing toxicity associated with conventional carriers.
Bicyclic peptide ligands bind to natural killer cell receptors, overcoming low tumor recognition by enhancing cytotoxicity.
Segmented peptide fragments inhibit SIRPα to enhance phagocytosis while avoiding off-target toxicity from full-length antibody Fc regions.
Coumarin and NBD fluorescent amino acids enable precise protein interaction measurements via Förster resonance energy transfer.
Oligonucleotide compounds bind pathogenic CUG repeats to disrupt MBNL1 sequestration, correcting splicing defects and restoring protein expression.
IgG-binding peptide mediates site-specific radioactive metal labeling on antibody Fc domain, reducing liver accumulation.
A cyclized peptide mimics transthyretin to bind amyloid-beta and protect neurons.
Replacing 1,3-dichloroacetone with 1,1-dichloroacetone solves the trade-off between low alkali resistance and poor IgG affinity in peptide production.