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Nerve growth factor ( NGF ), a member of the neurotrophin family, is known to regulate the development and survival of a select population of neurons through the binding and activation of the TrkA receptor. Elevated levels of  NGF  have been associated with painful pathologies such as diabetic neuropathy and fibromyalgia. However, completely inhibiting the  NGF  signal could hold significant side effects, such as those observed in a genetic condition called congenital insensitivity to pain and anhidrosis ( CIPA ). Previous methods of screening for  NGF ‐inhibitors used labeling techniques which have the potential to alter molecular interactions.  SPR  spectroscopy and  NGF ‐dependent cellular assays were utilized to identify a novel  NGF ‐inhibitor,  BVNP ‐0197 ( IC  50  = 90 nmol/L), the first  NGF ‐inhibitor described with a high nanomolar  NGF  inhibition efficiency. The present study utilizes molecular modeling flexible docking to identify a novel binding domain in the loop  II / IV  cleft of  NGF .

Nerve growth factor inhibitor with novel‐binding domain demonstrates nanomolar efficacy in both cell‐based and cell‐free assay systems