Dependence of benzyl alcohol loss on<i>C</i>‐terminal amino acid in tandem mass spectrometry of<i>N</i>‐protected tripeptides

Schwartz, Brenda L.; Erickson, Bruce W.; Bursey, Maurice M.; Marbury, G. Dean

doi:10.1002/oms.1210281013

Cited by 4 publications

(1 citation statement)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The different kinetic energy released from these decarboxylation reactions allowed the diastereomers to be discriminated from each other. Using unimolecular decomposition, another study showed that different diastereomers had different product ion abundances [98]. …”

Section: Analytical Techniques Used To Characterize Daacpsmentioning

confidence: 99%

Analysis of endogenous d-amino acid-containing peptides in Metazoa

2009

View full text Add to dashboard Cite

Peptides are chiral molecules with their structure determined by the composition and configuration of their amino acid building blocks. The naturally occurring amino acids, except glycine, possess two chiral forms. This allows the formation of multiple peptide diastereomers that have the same sequence. Although living organisms use L-amino acids to make proteins, a group of D-amino acid-containing peptides (DAACPs) has been discovered in animals that have at least one of their residues isomerized to the D-form via an enzyme-catalyzed process. In many cases, the biological functions of these peptides are enhanced due to this structural conversion. These DAACPs are different from those known to occur in bacterial cell wall and antibiotic peptides, the latter of which are synthesized in a ribosome-independent manner. DAACPs have now also been identified in a number of distinct groups throughout the Metazoa. Their serendipitous discovery has often resulted from discrepancies observed in bioassays or in chromatographic behavior between natural peptide fractions and peptides synthesized according to a presumed all-L sequence. Because this L-to-D post-translational modification is subtle and not detectable by most sequence determination approaches, it is reasonable to suspect that many studies have overlooked this change; accordingly, DAACPs may be more prevalent than currently thought. Although diastereomer separation techniques developed with synthetic peptides in recent years have greatly aided in the discovery of natural DAACPs, there is a need for new, more robust methods for naturally complex samples. In this review, a brief history of DAACPs in animals is presented, followed by discussion of a variety of analytical methods that have been used for diastereomeric separation and detection of peptides.

show abstract

Section: Analytical Techniques Used To Characterize Daacpsmentioning

confidence: 99%

Analysis of endogenous d-amino acid-containing peptides in Metazoa

2009

View full text Add to dashboard Cite

show abstract

Collisional‐activated decomposition of benzyloxycarbonyl‐protected tripeptide derivatives containing proline in fast atom bombardment mass spectrometry

Tsunematsu

Yamamoto

Isobe

1994

Org. Mass Spectrom.

View full text Add to dashboard Cite

The effect on the fragmentations of N-benzyloxycarbonyl-protected tripeptide ethyl esters due to the existence of L-proline in the gas phase was examined by the collisional-activated decomposition of the deprotonated molecule and the fragment ions produced by the cleavage of the tripeptide derivatives containing the neutral amino acids (L-alanine, L-leucine and L-phenylalanine) and L-proline, in which changes in both the numbers and positions of the prolyl residues were observed, in negative-ion fast atom bombardment mass spectrometry. The cleavage patterns of these ions in the collisional-activated decomposition mass spectra were observed to depend on the numbers and positions of prolyl residues in the peptide derivatives. These results indicate that the conformational differences in the peptide derivatives due to the existence of L-proline affect the decomposition of the ions containing the neutral amino acids in the gas phase.

show abstract

Analysis of endogenous D-amino acid-containing peptides in Metazoa

Bai¹,

Sheeley²,

Sweedler³

2009

Frontiers of Bioanalytical Chemistry

View full text Add to dashboard Cite

Peptides are chiral molecules with their structure determined by the composition and configuration of their amino acid building blocks. The naturally occurring amino acids, except glycine, possess two chiral forms. This allows the formation of multiple peptide diastereomers that have the same sequence. Although living organisms use L-amino acids to make proteins, a group of D-amino acidcontaining peptides (DAACPs) has been discovered in animals that have at least one of their residues isomerized to the D-form via an enzyme-catalyzed process. In many cases, the biological functions of these peptides are enhanced due to this structural conversion. These DAACPs are different from those known to occur in bacterial cell wall and antibiotic peptides, the latter of which are synthesized in a ribosome-independent manner. DAACPs have now also been identified in a number of distinct groups throughout the Metazoa. Their serendipitous discovery has often resulted from discrepancies observed in bioassays or in chromatographic behavior between natural peptide fractions and peptides synthesized according to a presumed all-L sequence. Because this L-to-D post-translational modification is subtle and not detectable by most sequence determination approaches, it is reasonable to suspect that many studies have overlooked this change; accordingly, DAACPs may be more prevalent than currently thought. Although diastereomer separation techniques developed with synthetic peptides in recent years have greatly aided in the discovery of natural DAACPs, there is a need for new, more robust methods for naturally complex samples. In this review, a brief history of DAACPs in animals is presented, followed by discussion of a variety of analytical methods that have been used for diastereomeric separation and detection of peptides.

show abstract

Dependence of benzyl alcohol loss onC‐terminal amino acid in tandem mass spectrometry ofN‐protected tripeptides

Cited by 4 publications

References 26 publications

Analysis of endogenous d-amino acid-containing peptides in Metazoa

Analysis of endogenous d-amino acid-containing peptides in Metazoa

Collisional‐activated decomposition of benzyloxycarbonyl‐protected tripeptide derivatives containing proline in fast atom bombardment mass spectrometry

Analysis of endogenous D-amino acid-containing peptides in Metazoa

Contact Info

Product

Resources

About