RPEP-00586 · 2000Alpha-MSH and its C-terminal tripeptide fragment KPV demonstrated direct antimicrobial activity against S. aureus, C. albicans, and E. coli, establishing a dual anti-inflammatory/antimicrobial function for this neuropeptide.
Catania, A; Cutuli, M; Garofalo, L; Carlin, A; Airaghi, L; Barcellini, W; Lipton, J M · In Vitro
RPEP-00588 · 2000Alpha-MSH and KPV demonstrated broad-spectrum antimicrobial activity including against MRSA and drug-resistant organisms, with an anti-Candida mechanism resembling amphotericin B membrane disruption.
Cutuli, M; Cristiani, S; Lipton, J M; Catania, A · In Vitro
RPEP-00594 · 2000Alpha-MSH modulates inflammation through melanocortin receptor-mediated inhibition of NF-κB signaling, reducing pro-inflammatory cytokines, fever, and immune activation in both peripheral tissues and the central nervous system.
Ichiyama, T; Sato, S; Okada, K; Catania, A; Lipton, J M · Review
RPEP-00820 · 2003KPV (alpha-MSH 11-13) reduced crystal-induced peritonitis as effectively as full-length alpha-MSH via systemic administration, with melanocortin receptor-independent anti-inflammatory activity at the inflammation site.
Getting, Stephen J; Schiöth, Helgi B; Perretti, Mauro · Animal Study
RPEP-00845 · 2003Alpha-MSH and KPV serve triple immune functions: anti-inflammatory (NF-κB inhibition, cytokine suppression), antimicrobial (direct pathogen killing), and immunomodulatory (melanocortin receptor-mediated immune cell regulation) — a comprehensive immune regulatory system.
Luger, Thomas A; Scholzen, Thomas E; Brzoska, Thomas; Böhm, Markus · Review
RPEP-00907 · 2004KPV inhibited NF-κB inflammatory signaling in human keratinocytes through a cAMP-independent mechanism, distinct from full-length alpha-MSH's classical cAMP-dependent MC1R signaling.
Elliott, Richard J; Szabo, Marika; Wagner, Mark J; Kemp, E Helen; MacNeil, Sheila; Haycock, John W · In Vitro
RPEP-01138 · 2006Dimeric KPV peptide (CKPV)2 inhibited endotoxin-induced host responses including fever, TNF-α/IL-6 release, and organ damage in mice, with enhanced anti-inflammatory potency compared to monomeric alpha-MSH — demonstrating improved efficacy through KPV dimerization.
Gatti, Stefano; Carlin, Andrea; Sordi, Andrea; Leonardi, Patrizia; Colombo, Gualtiero; Fassati, Luigi R; Lipton, James M; Catania, Anna · Animal Study
RPEP-01151 · 2006GKPV (alpha-MSH 10-13) immobilized on surfaces retained NF-κB inhibitory activity against TNF-α-stimulated inflammation in vitro, demonstrating that KPV-related peptides can function as bioactive anti-inflammatory coatings for medical devices and implants.
Kelly, J M; Moir, A J G; Carlson, K; Yang, Y; MacNeil, S; Haycock, J W · In Vitro
RPEP-01263 · 2007Alpha-MSH-derived peptides (KPV, ACTH fragments) constitute a new anti-inflammatory drug class operating through NF-κB inhibition, regulatory T-cell induction, and melanocortin receptor-dependent/independent pathways — applicable to IBD, arthritis, allergic, and neuroinflammatory diseases.
Luger, Thomas A; Brzoska, Thomas · Review