PIN inhibitory peptide

PIN inhibitory peptide (also known as Tat-PIN-I or Peptide I) is a cell-permeant synthetic peptide designed to disrupt the interaction between the Protein Inhibitor of Neuronal Nitric Oxide Synthase (PIN, also known as dynein light chain 8 or DYNLL1) and its cellular binding partners. Developed by researchers at the University of Montpellier and Uppsala University, the peptide consists of an optimized inhibitory sequence (IDVGIQVDWD) derived from the PIN-binding motif of neuronal nitric oxide synthase (nNOS), coupled to a cell-penetrating Tat-peptide sequence (GRKKRRQRRR) to facilitate intracellular delivery. By binding to the hydrophobic grooves of the DYNLL1 dimer, the peptide competitively blocks DYNLL1 from interacting with its physiological partners, including nNOS, myosin Va, and tubulin. In preclinical models, PIN inhibitory peptide has been utilized as a chemical biology tool to investigate the role of DYNLL1 in regulating glucose-induced insulin secretion in pancreatic beta cells and insulin-stimulated glucose uptake in skeletal muscle. Disruption of these interactions leads to decreased insulin secretion, increased tubulin polymerization, and impaired glucose transport, highlighting the role of DYNLL1 as a key modulator of cytoskeletal dynamics and metabolic homeostasis.

Other names

Peptide ITat-PIN inhibitory peptideTat-PIN-Icell-permeant PIN inhibitory peptide