PTD-DBM

PTD-DBM is a synthetic 25-amino-acid research peptide developed by Professor Kang-Yell Choi's lab at Yonsei University. It contains a protein transduction domain (PTD) fused to a dishevelled-binding motif (DBM) and functions by disrupting the inhibitory CXXC5–Dishevelled protein interaction to reactivate Wnt/β-catenin signaling in hair follicles. It has been studied topically and in combination with valproic acid for androgenetic alopecia and wound-induced hair neogenesis in rodent models.

CXXC5 is a zinc-finger protein that acts as a negative feedback regulator of the Wnt/β-catenin pathway by binding Dishevelled (Dvl), an upstream scaffold protein. Elevated CXXC5 expression in the balding scalp suppresses follicle regeneration by blocking Wnt target gene transcription. PTD-DBM contains an eight-arginine PTD sequence (RRRRRRRR) that enables membrane transduction and penetration into follicular cells, fused to a DBM segment (RKTGHQICKFRK) that competitively displaces CXXC5 from Dvl. Releasing this brake reactivates Wnt/β-catenin signaling, driving hair follicle stem cell proliferation, anagen phase extension, and wound-induced hair neogenesis. Combined treatment with valproic acid, a GSK-3β inhibitor that further amplifies Wnt/β-catenin signaling, produces additive hair regrowth in murine models.

Yonsei University preclinical studies published in the Journal of Investigative Dermatology (Choi et al.) demonstrated that topical PTD-DBM alone produced visible hair regrowth in C57BL/6 mice at levels comparable to minoxidil. Combined PTD-DBM plus valproic acid produced significantly greater hair follicle neogenesis than either agent alone, with new hair follicle counts exceeding vehicle control by over 2-fold. As of 2026, no human clinical trials have been published. A subsequent 2023 PMC study confirmed CXXC5 overexpression in androgenetic alopecia scalp biopsies, supporting target relevance in human disease.

Peptides commonly paired with PTD-DBM for synergistic effects.