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In recent years, the synthetic analogue elcatonin has been used successfully in the treatment of osteoporosis. During an investigation of synthetic strategies for the production of elcatonin, a number of peptide products were generated. These could be purified by liquid chromatography and were shown to have identical amino acid compositions. Investigation by fast atom bombardment-mass spectrometry revealed three of the peptides to have a common pseudomolecular ion but notably dissimilar fragmentation patterns. Further studies involving chemical modification, mass spectrometry and chromatographic separation showed these products to be novel depsipeptides, cyclized with an ester bond between either the serine or the threonine residue and the side chain of aminosuberic acid.
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K Penzes
January 1995,
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M Rogers, and
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K Penzes
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M Rogers, and
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J Varga, and
K Penzes
October 1982,
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M Rogers, and
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J Varga, and
K Penzes
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Biomedical & environmental mass spectrometry,
M Rogers, and
S Kelly, and
J Varga, and
K Penzes
September 1987,
Biomedical & environmental mass spectrometry,
M Rogers, and
S Kelly, and
J Varga, and
K Penzes
July 1990,
Biomedical & environmental mass spectrometry,
M Rogers, and
S Kelly, and
J Varga, and
K Penzes
May 1993,
Biological mass spectrometry,
M Rogers, and
S Kelly, and
J Varga, and
K Penzes
January 1993,
Methods in molecular biology (Clifton, N.J.),
M Rogers, and
S Kelly, and
J Varga, and
K Penzes
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Biomedical & environmental mass spectrometry,
M Rogers, and
S Kelly, and
J Varga, and
K Penzes
December 1987,
Analytical chemistry,
