Reference

Synthesis of a Highly Pure Lipid Core Peptide Based Self-Adjuvanting Triepitopic Group A Streptococcal Vaccine, and Subsequent Immunological Evaluation

All Rights Reserved.Some chemicals with cas registry numbers like 915129-07-6 and 84624-27-1 are also used. Synthesis of a Highly Pure Lipid Core Peptide Based Self-Adjuvanting Triepitopic Group A Streptococcal Vaccine, and Subsequent Immunological Evaluation. Moyle, Peter M.; Olive, Colleen; Ho, Mei-Fong; Good, Michael F.; Toth, Istvan (School of Pharmacy, University of Queensland, St. Lucia 4072, Australia). Journal of Medicinal Chemistry, 49(21), 6364-6370 (English) 2006 American Chemical Society. CODEN: JMCMAR. ISSN: 0022-2623. DOCUMENT TYPE: Journal CA Section: 63 (Pharmaceuticals) Section cross-reference(s): 1, 15, 34 We have developed a highly pure, self-adjuvanting, triepitopic Group A Streptococcal vaccine based on the lipid core peptide system, a vaccine delivery system incorporating lipidic adjuvant, carrier, and peptide epitopes into a single mol. entity. Vaccine synthesis was performed using native chem. ligation. Due to the attachment of a highly lipophilic adjuvant, addn. of 1% (w/v) sodium dodecyl sulfate was necessary to enhance peptide soly. in order to enable ligation. The vaccine was synthesized in three steps to yield a highly pure product (97.7% purity) with an excellent overall yield. S.c. immunization of B10.BR (H-2k) mice with the synthesized vaccine, with or without the addn. of complete Freund's adjuvant, elicited high serum IgG antibody titers against each of the incorporated peptide epitopes. .

A general method for preparation of peptides biotinylated at the carboxy terminus

A general method for preparation of peptides biotinylated at the carboxy terminus. Geahlen, Robert L.; Loudon, G. Marc; Paige, Lisa A.; Lloyd, David (Sch. Pharm. Pharmacal Sci., Purdue Univ., West Lafayette, IN 47907, USA). Anal. Biochem., 202(1), 68-70 (English) 1992. CODEN: ANBCA2. ISSN: 0003-2697. DOCUMENT TYPE: Journal CA Section: 34 (Amino Acids, Peptides, and Proteins) A method for the prepn. of a biotinylated resin that can be elongated by std. methods of solid-phase peptide synthesis to give peptides biotinylated at the carboxy terminus is described. This methodol. is particularly important for the prepn. fo biotinylated peptides in which a free amino terminus is required. Coupling of Ne-9-fluorenylmethoxycarbonyl(Fmoc)-Na-tert-butyloxycarbonyl(Boc)-L-ly sine to p-methylbenzhydrylamine resin, followed by removal of the Fmoc protecting group and reaction with (+)-biotin-4-nitrophenyl ester yielded Na-Boc-biocytin-p-methylbenzhydrylamine resin. The utility of this resin was tested by the synthesis of a biotinylated peptide, Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg-biocytin-NH2, for use as an in vitro substrate for myristoyl-CoA:protein N-myristoyltransferase (NMT), the enzyme that catalyzes protein N-myristoylation. 84624-27-1 and 33755-53-2 which are cas registry numbers of substances are two of reagents here. Anal. of the peptide deriv. by HPLC and mass spectrometry revealed a single major product of the expected mass, indicating that the biotin group survived cleavage and deprotection with HF. The biotinylated peptide served as a substrate for NMT, and the resulting myristoylated peptide could be quant. recovered by adsorption to immobilized avidin. .