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C W Chung

Publications and source records attributed to C W Chung.

43 records · Page 3Linked to original sources

Sensitization potentials and immunologic specificities of neomycins.

The use of sensitization indices for expressing allergenic skin reactions in guinea pigs is described. The method is convenient for comparing allergens and cross-reacting substances and permits the use of both irritating and nonirritating challenge concentrations of allergens. It also permits determination of both optimal reading time and challenge concentrations for each experiment. By this technique commercial neomycin complex, neamine (neomycin A), neomycin B, neomycin C, and streptomycin were found to be allergenic in guinea pigs via intradermal (id) and foot-pad (fp) immunizations. The immunizing emulsion consisted of an allergen and an adjuvant containing Mycobacterium butyricum (MB) or Mycobacterium tuberculosis H37Ra (Ra). The adjuvant MB was as effective as Ra by the id route, but inferior to Ra by the fp route. The cross-reactivity of neomycin C was generally greater than neomycin B in guinea pigs sensitized to neamine, neomycin B, neomycin C, or streptomycin. In guinea pigs sensitized to neomycin complex by repeated immunizations, neomycins A, B, and C were effective elicitors of skin reactions, whereas the N-acetylated derivatives of the components failed to cause reactions. This finding is interpreted to mean that the amino groups of the aminoglycosides are the coupling sites to host proteins in the processes of sensitization and elicitation of skin reactions in vivo.

Adjuvants, Immunologic↗

Conformational analysis of neuropeptide Y segments by CD, NMR spectroscopy and restrained molecular dynamics.

Neuropeptide Y (NPY), a peptide amide comprising 36 residue has been shown to act as a potent vasoconstrictor. In order to shed light on the structural requirements for the biological activities with respect to the different prerequisites for affinity to the NPY receptor subtypes Y1 and Y2, in the present study the syntheses and conformational analyses of two C-terminal segments, NPY(18-36) and NPY(13-36), are described. The results obtained by CD measurements, two-dimensional NMR spectroscopy and a conformational refinement of the NMR-derived structure by molecular mechanics stimulations support the findings of previously published structure-activity relationship studies for biologically active and selective compounds. In particular, the alpha-helical conformation as well as an appropriate exposure of the side chains of the critical C-terminal dipeptide within NPY(18-36) are in agreement with the prerequisites proposed for Y2 receptor binding of that segment.

Amino Acid Sequence↗