{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Piekarz AD"],"funding":["NCRR NIH HHS","NIDA NIH HHS","NINDS NIH HHS"],"pagination":["54"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3502107"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["8"],"pubmed_abstract":["<h4>Background</h4>The ubiquity of protein-protein interactions in biological signaling offers ample opportunities for therapeutic intervention. We previously identified a peptide, designated CBD3, that suppressed inflammatory and neuropathic behavioral hypersensitivity in rodents by inhibiting the ability of collapsin response mediator protein 2 (CRMP-2) to bind to N-type voltage-activated calcium channels (CaV2.2) [Brittain et al. Nature Medicine 17:822-829 (2011)].<h4>Results and discussion</h4>Here, we utilized SPOTScan analysis to identify an optimized variation of the CBD3 peptide (CBD3A6K) that bound with greater affinity to Ca²⁺ channels. Molecular dynamics simulations demonstrated that the CBD3A6K peptide was more stable and less prone to the unfolding observed with the parent CBD"],"journal":["Molecular pain"],"pubmed_title":["CRMP-2 peptide mediated decrease of high and low voltage-activated calcium channels, attenuation of nociceptor excitability, and anti-nociception in a model of AIDS therapy-induced painful peripheral neuropathy."],"pmcid":["PMC3502107"],"funding_grant_id":["R01 NS049136","NS049136-06","DA026040-04","RR025761"],"pubmed_authors":["Piekarz AD","Wang B","Wang R","Ripsch MS","Khanna R","Due MR","Vasko MR","Khanna M","White FA","Meroueh SO"],"additional_accession":[]},"is_claimable":false,"name":"CRMP-2 peptide mediated decrease of high and low voltage-activated calcium channels, attenuation of nociceptor excitability, and anti-nociception in a model of AIDS therapy-induced painful peripheral neuropathy.","description":"<h4>Background</h4>The ubiquity of protein-protein interactions in biological signaling offers ample opportunities for therapeutic intervention. We previously identified a peptide, designated CBD3, that suppressed inflammatory and neuropathic behavioral hypersensitivity in rodents by inhibiting the ability of collapsin response mediator protein 2 (CRMP-2) to bind to N-type voltage-activated calcium channels (CaV2.2) [Brittain et al. Nature Medicine 17:822-829 (2011)].<h4>Results and discussion</h4>Here, we utilized SPOTScan analysis to identify an optimized variation of the CBD3 peptide (CBD3A6K) that bound with greater affinity to Ca²⁺ channels. Molecular dynamics simulations demonstrated that the CBD3A6K peptide was more stable and less prone to the unfolding observed with the parent CBD","dates":{"release":"2012-01-01T00:00:00Z","publication":"2012 Jul","modification":"2026-04-07T20:46:14.688Z","creation":"2026-04-07T17:47:08.12Z"},"accession":"S-EPMC3502107","cross_references":{"pubmed":["22828369"],"doi":["10.1186/1744-8069-8-54"]}}