Mass spectrometric evaluation of synthetic peptides as primary structure models for peptide and protein deamidation.
Solid-phase peptide synthesis and deamidation measurements using a novel mass spectrometric technique were carried out for 94 model asparaginyl peptides from 3 to 13 residues in length. Deamidation rates of these peptides in pH 7.4, 37.0 degrees C, 0.15 M Tris-HCl buffer were measured and evaluated. It was found that they validate the use of pentapeptide models as surrogates for the primary sequence dependence of peptide and protein deamidation rates and the discovery by difference of secondary, tertiary and quaternary structure effects. Deamidation of the pentapeptide models, compared with that of longer peptides of more intricate structure, is discussed, and the application of this technique to deamidation measurement of intact proteins is demonstrated.
Robinson
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NE
Chemistry Department, California Institute of Technology, USA.
Robinson
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AB
Merrifield
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RB
D000577:Amides / Q000737:chemistry*; D000595:Amino Acid Sequence; D000818:Animals; D003641:Deamination; D005634:Fructose-Bisphosphate Aldolase / Q000737:chemistry; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D009132:Muscles / Q000378:metabolism; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry*; D011817:Rabbits; D013997:Time Factors
D000577:Amides; D009842:Oligopeptides; D010446:Peptide Fragments; D005634:Fructose-Bisphosphate Aldolase