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Ridwan R., Kiptoo P., Kobayashi N., Weir S., Hughes M., Williams T., Soegianto R., Siahaan T.J.
24482358700;6505587917;57199477164;57206314064;35074090600;7404172537;6507142727;7005696163;
Antigen-specific suppression of experimental autoimmune encephalomyelitis by a novel bifunctional peptide inhibitor: Structure optimization and pharmacokinetics
2010
Journal of Pharmacology and Experimental Therapeutics
332
3
1136
1145
18
Department of Pharmaceutical Chemistry, University of Kansas, Simons Research Laboratories, 2095 Constant Avenue, Lawrence, KS 66047, United States; Mass Spectrometry Laboratory, University of Kansas, Lawrence, KS, United States; Astellas Pharma Inc., Yaizu, Shizuoka, Japan; Cancer Center, University of Kansas, Kansas City, KS, United States; Faculty of Medicine, University of Indonesia, Jakarta, Indonesia
Ridwan, R., Department of Pharmaceutical Chemistry, University of Kansas, Simons Research Laboratories, 2095 Constant Avenue, Lawrence, KS 66047, United States; Kiptoo, P., Department of Pharmaceutical Chemistry, University of Kansas, Simons Research Laboratories, 2095 Constant Avenue, Lawrence, KS 66047, United States; Kobayashi, N., Astellas Pharma Inc., Yaizu, Shizuoka, Japan; Weir, S., Cancer Center, University of Kansas, Kansas City, KS, United States; Hughes, M., Cancer Center, University of Kansas, Kansas City, KS, United States; Williams, T., Mass Spectrometry Laboratory, University of Kansas, Lawrence, KS, United States; Soegianto, R., Faculty of Medicine, University of Indonesia, Jakarta, Indonesia; Siahaan, T.J., Department of Pharmaceutical Chemistry, University of Kansas, Simons Research Laboratories, 2095 Constant Avenue, Lawrence, KS 66047, United States
The objective of this study was to optimize the in vivo activity of proteolipid protein (PLP)-bifunctional peptide inhibitor (BPI) molecule to suppress experimental autoimmune encephalomyelitis (EAE) in SJL/J mice and evaluate pharmacokinetic profiles of PLP-BPI. PLP-BPI is constructed via conjugation of myelin PLP139-151 with CD11a237-246-derived peptide (LABL) via a spacer. The hypothesis is that PLP-BPI binds simultaneously to major histocompatibility complex-II and intercellular adhesion molecule-1 on the antigen-presenting cell (APC) and inhibits the formation of the immunological synapse during T-cell and APC interactions. In this study, the structure of BPI was modified by varying the spacer and was evaluated in the EAE model. Intravenous injections of BPI derivatives inhibited the onset, severity, and incidence of EAE more effectively and induced a lower incidence of anaphylaxis than that produced by unmodified PLP-BPI. As anticipated, production of interleukin-17, a proinflammatory cytokine commonly found in elevated levels among multiple sclerosis (MS) patients, was significantly lower in Ac-PLP-BPI-PEG6- or Ac-PLP-BPI-NH2-2-treated mice than in phosphate-buffered saline-treated mice. These results suggest that BPI-type molecules can be modified to achieve more efficient and better tolerated BPI-based derivatives for the treatment of MS. Copyright © 2010 by The American Society for Pharmacology and Experimental Therapeutics.
aminocaproic acid; CD11a antigen [237-246]; epitope; intercellular adhesion molecule 1; macrogol 6000; myelin; phosphate buffered saline; protein inhibitor; proteolipid bifunctional peptide inhibitor; proteolipid protein [139-515]; unclassified drug; allergic encephalomyelitis; amino acid sequence; amino terminal sequence; animal experiment; animal model; antigen presenting cell; antigen specificity; area under the curve; article; cell interaction; comparative study; controlled study; cytokine production; disease severity; drug activity; drug inhibition; drug protein binding; drug structure; female; in vivo study; major histocompatibility complex; male; morbidity; mouse; multiple sclerosis; nonhuman; priority journal; rat; T lymphocyte; Anaphylaxis; Animals; Antigens, CD11; Encephalomyelit
00223565
JPETA
20026673
Article
Q1