Amino acid sequence and D/L‐configuration determination methods for D‐amino acid‐containing peptides in living organisms

Abstract

D-amino acid-containing peptides with biological activities have been isolated from invertebrates and amphibians, and partial racemization of amino acid residues in mammalian peptides associated with aging and diseases have been discussed. Here, we review the amino acid configuration determination methods in these peptides and recent progress of simultaneous determination method for sequence and configuration of amino acid residues. The applicability of C-terminus sequence analysis and mass spectrometry to configuration determination of amino acids is also discussed.

Measuring d-amino acid-containing neuropeptides with capillary electrophoresis

“…The primary techniques used for the study of peptides containing amino acids in the D-form include HPLC separation of intact peptides, N-terminal sequencing, and immunohistochemistry. 10 HPLC has the advantage of purifying peptides with multi-step separations, but the limitation is that it usually needs a larger sample in comparison to CE. Consequently, it is hard to perform single cell analyses.…”

Experimental strategies for the analysis of d-amino acid containing peptides in crustaceans: A review

“…This approach, though technically not very straightforward and which needs nanomolar amounts of peptide (review in [18]), still remains the most accurate and reliable method to determine the stereochemistry of AA residues in peptides.…”

Aspartic acid racemization of root dentin used for dental age estimation in a Polish population sample

“…It has two enantiomers (optical isomers), which are mirror reflections of each other. Those enantiomers, L and D, can rotate in the plane of polarized light in opposite directions (left or right), which converts them into a racemic mixture [ 8 , 9 ]. In other words, Asp racemization is a non-enzymatic reaction that causes age-dependent accumulation of a detectable protein product [ 10 – 12 ].…”