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NMR Identification of the Formic Acid‐Modified Residue in Alzheimer's Amyloid Protein
Author(s) -
Klunk William E.,
Xu ChongJun,
Pettegrew Jay W.
Publication year - 1994
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1994.62010349.x
Subject(s) - formic acid , chemistry , residue (chemistry) , covalent bond , peptide , serine , chemical modification , formate , solubilization , amyloid (mycology) , combinatorial chemistry , biochemistry , organic chemistry , enzyme , inorganic chemistry , catalysis
The β/A4‐amyloid protein (β/A4) and many synthetic fragments of this protein have proved to be very difficult to solubilize, leading to the use of relatively harsh chemical methods, most notably, formic acid. This treatment has previously been shown to cause a covalent modification of this peptide. In this study, one‐ and two‐dimensional NMR techniques are used to show that the nature of this covalent modification is formation of a formate ester to a serine residue. This finding is consistent with our previously reported kinetic studies of formic acid‐induced modification ofβ / A4 and further illustrates the potential danger of solubilizing fragments of β/A4 in formic acid. Alternative methods of solubilization are discussed.