Circular dichroism (CD) studies on biological activity of mast cell degranulating (MCD) peptide analogs.
Analogs of MCD peptide were synthesized by solid-phase methods. Positive charges were deleted at the N-and/or C-terminus, including the helical portion of the molecule. Four peptides were prepared by removing residues 16-18 (Arg-Lys-Ile), 1-2 (Lys), 1-2 and 16-18 and by acetylation of the amino end (Ile). Analogs were tested on mast cells for histamine-releasing activity. Although the helicity of these derivatives, determined by circular dichroism (CD), was not significantly different from the native MCD peptide, two analogs with C-terminal deletions showed a 5- to 10-fold decrease in activity. These findings suggest that the C-terminus is more important than the N-terminus in determining bioactivity of MCD peptide.
Buku
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A
Department of Physiology and Biophysics, Mount Sinai School of Medicine, New York, NY.
Mirza
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U
Polewski
K
K
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D006636:Histamine Release / Q000187:drug effects; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis / Q000494:pharmacology* / Q000502:physiology; D017433:Protein Structure, Secondary
D010455:Peptides; C008331:mast cell degranulating peptide