Conformational study of a short Pertussis toxin T cell epitope incorporated in a multiple antigen peptide template by CD and two-dimensional NMR. Analysis of the structural effects on the activity of synthetic immunogens.

The immunogenic efficacy of multiple antigen peptides, MAPs, i.e. branched molecules in which multiple copies of a given immunogenic peptide are attached on a scaffold of lysine residues via both alpha and epsilon linkages, has been repeatedly demonstrated, but little is known about the structural arrangement of these peptide constructs.

Side reactions in solid phase synthesis of histidine-containing peptides. Characterization of two major impurities by sample displacement chromatography and FAB-MS.

The flow-polyamide synthesis of a histidine-containing sequence (Ac-YDNVLDHLTGR) produced two major impurities which were isolated through Sample Displacement Chromatography and characterized by Fast Atom Bombardment-mass analysis. The impurities correspond to the sequence Ac-YDNVLDH, and to a peptide with the Asp residue cyclized to a succinimide. The latter side-reaction took place during the acetylation procedure, and demands attention where capping procedures are planned in the synthesis of Asp-His sequences.

Application of capillary zone electrophoresis to the characterization of multiple antigen peptides.

Capillary zone electrophoresis (CZE) was applied to the analysis of a recently described class of synthetic branched peptides, multiple antigen peptides (MAPs). In comparison with high-performance liquid chromatography (HPLC), CZE showed superior resolution of minor impurities in samples of MAPs obtained by preparative chromatography. MAPs that differed only in the substitution of uncharged residues (Ala-Ser) could be separated by the addition of organic solvents (acetonitrile, methanol, ethanol) to the aqueous background electrolyte.

Toward the elucidation of the mechanism of attachment and entry of malaria sporozoites into cells: synthetic polypeptides from the circumsporozoite protein of Plasmodium falciparum bind Ca2+ and interact with model phospholipid membranes.

Through the joint use of CD, Fourier transform ir (FTIR), and attenuated total reflectance FTIR we have found that synthetic polypeptide models of the Plasmodium falciparum circumsporozoite (CS) protein repeat domain bind calcium ions in helicogenic environments. Ca(2+)-(NANP)n complexes (n greater than or equal to 20) interact vectorially with model phospholipid membranes orienting their polypeptide axes preferentially along those of the lipid acyl chains. It is proposed that the P.

Multiple antigen peptides (MAPs) as candidate vaccines against malaria.

Multiple Antigen Peptides (MAPs), branched molecules where multiple copies of a desired antigenic sequence are assembled on a small peptide core, have been recently described as an alternative approach to the synthesis of high molecular weight immunogens. In comparison with conventional peptide-carrier conjugates, the MAPs show several advantages, including chemical unambiguity and ease of synthesis. A MAP based on the sequence of the repetitive domain of P.

A multiple antigen peptide from the repetitive sequence of the Plasmodium malariae circumsporozoite protein induces a specific antibody response in mice of various H-2 haplotypes.

The major repetitive epitopes of the surface circumsporozoite (CS) protein of malaria sporozoites represent candidates for the development of subunit vaccines against malaria. However, previous experimental work has shown that repetitive peptides from the CS proteins of Plasmodium falciparum, P. vivax, P.