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Fine Molecular Specificity of Linear and Assembled Antibody Binding Sites in HIV-1 p24 (1991)

HAAHEIM, L. R. ; MASKELL, J. P ; MASCAGNI, P. ; [et al.]

Oxford, UK : Blackwell Publishing Ltd

Scandinavian journal of immunology 34 (1991), S. 0

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ISSN: 1365-3083

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Medicine

Notes: A set of seven murine monoclonal antibodies were generated against a chemically synthesized 11-kDa 104-mer peptide covering the C-terminal residues 270-373 of the p24g.it; protein (HIV-IBRU strain). All monoclonal antibodies recognized HIV-LMN infected MOLT? cells by fluorescence und gave positive Western blot signals with viral gag peptides [p55 and/or p24), Oligopeptide binding regions were located with competitive enzyme-linked immunosorbent assays. Detailed epitope scanning analyses (the Geysen technique) were performed by serological testing of the monoclonal antibodies against 99 overlapping hexapeptides which corresponded to the entire 104-mer region. The antibodies bound to p24 peptide sequences located within the 275 2y3 and 351 36S regions. One antibody (LH 104-B) which reacted with residues 357-362 bound lo p55 alone. In contrast another antibody (LH 104–1). which recognized the residues 358–363. i.e. with five out of six residues in common with antibody LIIKM-B for its epitope region, reacted exclusively with p24.At least two of the antibodies (LH104-C and -A) which bound to p24 alone, apparently recognized conformational epitopes, They gave positive reactions with the regions 288—293/351–356 and 284–289/351–356, respectively.This work shows that chemical synthesis of large peptides is a viable alternative approach to immunochemical studies of viral proteins.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1111/j.1365-3083.1991.tb01555.x

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Conformational analysis of two cyclic disulfide peptides (1991)

García-Echeverría, C. ; Siligardi, G. ; Mascagni, P. ; [et al.]

New York : Wiley-Blackwell

Biopolymers 31 (1991), S. 835-843

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ISSN: 0006-3525

Keywords: Chemistry ; Polymer and Materials Science

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Chemistry and Pharmacology

Notes: Complete nmr and CD studies of two cyclic tetrapeptides with disulfide bonds, 1 and 2 bonds have been carried out in different solvents to investigate the formation and stabilization of β-turn structures and to determine the stereochemistry of the disulfide linkage. Both peptides have three-dimensional structures with a type II β-turn, as derived from quantitative nuclear Overhauser effect data. The combined use of CD and nmr indicates that the dihedral angle of the disulfide bridge is different in the two peptides, although the chirality is maintained.

Additional Material: 6 Ill.