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Collapse of Homochirality of Amino Acids in Proteins from Various Tissues during Aging
Author(s) -
Fujii Noriko,
Kaji Yuichi,
Fujii Norihiko,
Nakamura Tooru,
Motoie Ryota,
Mori Yuhei,
Kinouchi Tadatoshi
Publication year - 2010
Publication title -
chemistry and biodiversity
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.427
H-Index - 70
eISSN - 1612-1880
pISSN - 1612-1872
DOI - 10.1002/cbdv.200900337
Subject(s) - homochirality , chemistry , amino acid , abiogenesis , astrobiology , biochemistry , biophysics , biology
Abstract Prior to the emergence of life, it is believed that only L ‐amino acids were selected for formation of proteins, and that D ‐amino acids were eliminated on the primitive Earth. Whilst homochirality is essential for life, recently the occurrence of proteins containing D ‐ β ‐aspartyl (Asp) residues from various tissues of elderly subjects has been reported. Here, we discuss the presence of D ‐ β ‐Asp‐containing proteins in the lens, ciliary body, drusen, and sclera of the eye, skin, cardiac muscle, blood vessels of the lung, chief cells of the stomach, longitudinal and circular muscles of the stomach, and small and large intestines. Since the D ‐ β ‐Asp residue occurs through a succinimide intermediate, this isomer may potentially be generated in proteins more easily than initially thought. UV Rays and oxidative stress can accelerate the formation of the D ‐ β ‐Asp residue in proteins.