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Generation of enantiomeric amino acids during acid hydrolysis of peptides detected by the liquid chromatography/tandem mass spectroscopy.
Chem Biodivers. 2010 Jun; 7(6):1644-50.CB

Abstract

The number of reports indicating the occurrence of D-amino acids in various proteins and natural peptides is increasing. For a usual detection of peptidyl D-amino acids, proteins or peptides are subjected to acid hydrolysis, and the products obtained are analyzed after cancellation of the effect of amino acid racemization during the hydrolysis. However, this method does not seem reliable enough to determine the absence or presence of a small amount of innate D-amino acids. We introduce a modification of an alternative way to distinguish true innate D-amino acids from those artificially generated during hydrolysis incubation. When model peptides (L-Ala)(3), D-Ala-(L-Ala)(2) are hydrolyzed in deuterated hydrochloric acid (DCl), only newly generated D-amino acids are deuterated at the alpha-H-atom. Both innate D-amino acids and artificially generated ones are identified by the combination of high-performance liquid chromatography and liquid chromatography/tandem mass spectrometry equipped with a chiral column. When a peptide containing D-Phe residues was analyzed by this method, the hydrolysis-induced conversion to L-Phe was similarly identified.

Authors+Show Affiliations

Department of Biotechnology, Graduate School of Agricultural and Life Sciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

20564678

Citation

Miyamoto, Tetsuya, et al. "Generation of Enantiomeric Amino Acids During Acid Hydrolysis of Peptides Detected By the Liquid Chromatography/tandem Mass Spectroscopy." Chemistry & Biodiversity, vol. 7, no. 6, 2010, pp. 1644-50.
Miyamoto T, Sekine M, Ogawa T, et al. Generation of enantiomeric amino acids during acid hydrolysis of peptides detected by the liquid chromatography/tandem mass spectroscopy. Chem Biodivers. 2010;7(6):1644-50.
Miyamoto, T., Sekine, M., Ogawa, T., Hidaka, M., Homma, H., & Masaki, H. (2010). Generation of enantiomeric amino acids during acid hydrolysis of peptides detected by the liquid chromatography/tandem mass spectroscopy. Chemistry & Biodiversity, 7(6), 1644-50. https://doi.org/10.1002/cbdv.200900309
Miyamoto T, et al. Generation of Enantiomeric Amino Acids During Acid Hydrolysis of Peptides Detected By the Liquid Chromatography/tandem Mass Spectroscopy. Chem Biodivers. 2010;7(6):1644-50. PubMed PMID: 20564678.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Generation of enantiomeric amino acids during acid hydrolysis of peptides detected by the liquid chromatography/tandem mass spectroscopy. AU - Miyamoto,Tetsuya, AU - Sekine,Masae, AU - Ogawa,Tetsuhiro, AU - Hidaka,Makoto, AU - Homma,Hiroshi, AU - Masaki,Haruhiko, PY - 2010/6/22/entrez PY - 2010/6/22/pubmed PY - 2010/10/22/medline SP - 1644 EP - 50 JF - Chemistry & biodiversity JO - Chem Biodivers VL - 7 IS - 6 N2 - The number of reports indicating the occurrence of D-amino acids in various proteins and natural peptides is increasing. For a usual detection of peptidyl D-amino acids, proteins or peptides are subjected to acid hydrolysis, and the products obtained are analyzed after cancellation of the effect of amino acid racemization during the hydrolysis. However, this method does not seem reliable enough to determine the absence or presence of a small amount of innate D-amino acids. We introduce a modification of an alternative way to distinguish true innate D-amino acids from those artificially generated during hydrolysis incubation. When model peptides (L-Ala)(3), D-Ala-(L-Ala)(2) are hydrolyzed in deuterated hydrochloric acid (DCl), only newly generated D-amino acids are deuterated at the alpha-H-atom. Both innate D-amino acids and artificially generated ones are identified by the combination of high-performance liquid chromatography and liquid chromatography/tandem mass spectrometry equipped with a chiral column. When a peptide containing D-Phe residues was analyzed by this method, the hydrolysis-induced conversion to L-Phe was similarly identified. SN - 1612-1880 UR - https://www.unboundmedicine.com/medline/citation/20564678/Generation_of_enantiomeric_amino_acids_during_acid_hydrolysis_of_peptides_detected_by_the_liquid_chromatography/tandem_mass_spectroscopy_ L2 - https://doi.org/10.1002/cbdv.200900309 DB - PRIME DP - Unbound Medicine ER -