LNSMGQD

The tandem peptide containing LNSMGQD (20 μM; 30 min) selectively enhances the homophilic binding of Dsg2 under cell-free conditions, and reverses the inhibitory effect of L-tryptophan without affecting E-cadherin binding^[1].
The tandem peptide containing LNSMGQD (20 μM; 24 h) prevents TNF-α-induced loss of intercellular adhesion and increase in cell permeability in CaCo2 and HCT116 intestinal epithelial cells^[1].
The tandem peptide containing LNSMGQD (20 μM; 24 h) blocks the TNF-α-induced upregulated expression of the pore-forming tight junction protein claudin-2 in intestinal epithelial CaCo2 cells, and maintains the junctional localization of Dsg2 and claudin-1^[1].
LNSMGQD (200 μM; 24 h) disrupts intercellular adhesion of human keratinocyte HaCaT cells in dispase-based dissociation assays and induces keratin filament contraction^[2].
LNSMGQD (200 μM; 30 min) induces phosphorylation of p38 MAPK in human keratinocyte HaCaT cells^[2].
LNSMGQD (40 μM; 1 h) directly interferes with the binding sites involved in homophilic and heterophilic desmoglein 2 interactions to reduce the binding probability, without altering the single-molecule unbinding force^[3].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.