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

Soyez, Daniel; Toullec, Jean‐Yves; Montagné, Nicolas; Ollivaux, Céline

doi:10.1016/j.jchromb.2011.03.032

Cited by 13 publications

(19 citation statements)

References 45 publications

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“…Bonferroni post hoc test is as follows: **, p Ͻ 0.01; ***, p Ͻ 0.001. experiment, and this difference can be manifested as different branching ratios among product ions. It has been shown that several different MS techniques can be used to probe this thermochemical difference between diastereomers (34,61,62,(72)(73)(74). We have also shown that simultaneous identification and characterization of potential DAACPs by MALDI-TOF/ TOF MS can be applied to distinguish D-isomer peptides in biological samples as small as individual neurons (38).…”

Section: Approaches For Identifying Daacps In Biological Tissuementioning

confidence: 89%

“…Homology searches that exploited structural and functional similarities between prohormone sequences in other species (75) allowed us to generate a hypothesis for the existence of two Aplysia putative DAACPs encoding the prohormones GdFFD and YdAEFLa. Prior to MS characterization, we confirmed the expression and distribution of these prohormones in the CNS by molecular techniques and investigated their final gene products in isolated neurons using proven MALDI-TOF/TOF MS. We took advantage of the distinct fragmentation patterns that can arise between peptide epimers using both MALDI MS/MS-and LC-ESI MS/MSbased approaches (34,38,61,73,74) to distinguish DAACPs and their all L-peptide counterparts. Our identification of GdFFD in Aplysia, similar to achatin-I (GdFAD) in Achatina, validates our homology-based MS approach as being effective for identifying novel DAACPs in related animals.…”

Section: Approaches For Identifying Daacps In Biological Tissuementioning

confidence: 99%

“…More-over, methods that are compatible with small quantities of tissue samples are desirable as neuropeptide studies oftentimes are sample limited. Second, although DAACPs have been shown to be more bioactive in the CNS in several animals (1,34), it is not known how D-amino acid-containing neuropeptides might ultimately act on a specific neural circuit to affect network output and behavior. In fact, to the best of our knowledge, no studies have examined the effects of DAACPs on a defined neural circuit, likely due to the limited information on well defined neural circuits in most species.…”

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confidence: 99%

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Characterization of GdFFD, a d-Amino Acid-containing Neuropeptide That Functions as an Extrinsic Modulator of the Aplysia Feeding Circuit

Bai

Livnat

Romanova

et al. 2013

Journal of Biological Chemistry

108

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Background: L-to-D conversion of an amino acid in a neuropeptide can be required for bioactivity. Results: A new D-amino acid-containing peptide (DAACP), GdFFD, shows stereospecific bioactivity in the feeding circuit. Conclusion: Our findings broaden the importance of this unusual post-translational modification, providing new methods to accelerate DAACP discovery. Significance: GdFFD is the first DAACP showing bioactivity in a well defined circuit.

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Section: Approaches For Identifying Daacps In Biological Tissuementioning

confidence: 89%

Section: Approaches For Identifying Daacps In Biological Tissuementioning

confidence: 99%

mentioning

confidence: 99%

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Characterization of GdFFD, a d-Amino Acid-containing Neuropeptide That Functions as an Extrinsic Modulator of the Aplysia Feeding Circuit

Bai

Livnat

Romanova

et al. 2013

Journal of Biological Chemistry

108

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“… 4 Generally, the targeted approaches for discovery of endogenous DAACPs include two steps: screening DAACP candidates in biological samples and then localizing d -amino acid residues. 2 , 5 Many new DAACPs were found by observing the differences in biological activity or chromatographic retention time between synthetic peptides and naturally occurring peptides. 2 − 5 In addition, immunoassays based on conformational antibodies have been successfully used to screen DAACPs at the tissue and cellular level.…”

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confidence: 99%

Site-Specific Characterization of d-Amino Acid Containing Peptide Epimers by Ion Mobility Spectrometry

et al. 2014

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Traditionally, the d-amino acid containing peptide (DAACP) candidate can be discovered by observing the differences of biological activity and chromatographic retention time between the synthetic peptides and naturally occurring peptides. However, it is difficult to determine the exact position of d-amino acid in the DAACP candidates. Herein, we developed a novel site-specific strategy to rapidly and precisely localize d-amino acids in peptides by ion mobility spectrometry (IMS) analysis of mass spectrometry (MS)-generated epimeric fragment ions. Briefly, the d/l-peptide epimers were separated by online reversed-phase liquid chromatography and fragmented by collision-induced dissociation (CID), followed by IMS analysis. The epimeric fragment ions resulting from d/l-peptide epimers exhibit conformational differences, thus showing different mobilities in IMS. The arrival time shift between the epimeric fragment ions was used as criteria to localize the d-amino acid substitution. The utility of this strategy was demonstrated by analysis of peptide epimers with different molecular sizes, [d-Trp]-melanocyte-stimulating hormone, [d-Ala]-deltorphin, [d-Phe]-achatin-I, and their counterparts that contain all-l amino acids. Furthermore, the crustacean hyperglycemia hormones (CHHs, 8.5 kDa) were isolated from the American lobster Homarus americanus and identified by integration of MS-based bottom-up and top-down sequencing approaches. The IMS data acquired using our novel site-specific strategy localized the site of isomerization of l- to d-Phe at the third residue of the CHHs from the N-terminus. Collectively, this study demonstrates a new method for discovery of DAACPs using IMS technique with the ability to localize d-amino acid residues.

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“…The analysis of d - amino acids within polypeptides poses a challenge, 13 mainly due to two limitations: first, although Edman degradation gives rise to chiral phenylthiohydantoin amino acid derivatives, for the resolution of the enantiomers, chiral media are required; 14 second, stereoisomerisation does not lead to any detectable mass differences. Moreover, fragment masses are identical for all stereoisomers in tandem MS experiments, which nowadays is the commonly used sequencing method.…”

Section: Introductionmentioning

confidence: 99%

MALDI TOF/TOF-Based Approach for the Identification of d- Amino Acids in Biologically Active Peptides and Proteins

et al. 2016

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Several biologically active peptides contain a d- amino acid in a well-defined position, which is position 2 in all peptide epimers isolated to date from vertebrates and also some from invertebrates. The detection of such D- residues by standard analytical techniques is challenging. In tandem mass spectrometric (MS) analysis, although fragment masses are the same for all stereoisomers, peak intensities are known to depend on chirality. Here, we observe that the effect of a d- amino acid in the second N-terminal position on the fragmentation pattern in matrix assisted laser desorption time-of-flight spectrometry (MALDI-TOF/TOF MS) strongly depends on the peptide sequence. Stereosensitive fragmentation (SF) is correlated to a neighborhood effect, but the d- residue also exerts an overall effect influencing distant bonds. In a fingerprint analysis, multiple peaks can thus serve to identify the chirality of a sample in short time and potentially high throughput. Problematic variations between individual spots could be successfully suppressed by cospotting deuterated analogues of the epimers. By identifying the [d-Leu2] isomer of the predicted peptide GH-2 (gene derived bombininH) in skin secretions of the toad Bombina orientalis, we demonstrated the analytical power of SF-MALDI-TOF/TOF measurements. In conclusion, SF-MALDI-TOF/TOF MS combines high sensitivity, versatility, and the ability to complement other methods.

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

Cited by 13 publications

References 45 publications

Characterization of GdFFD, a d-Amino Acid-containing Neuropeptide That Functions as an Extrinsic Modulator of the Aplysia Feeding Circuit

Characterization of GdFFD, a d-Amino Acid-containing Neuropeptide That Functions as an Extrinsic Modulator of the Aplysia Feeding Circuit

Site-Specific Characterization of d-Amino Acid Containing Peptide Epimers by Ion Mobility Spectrometry

MALDI TOF/TOF-Based Approach for the Identification of d- Amino Acids in Biologically Active Peptides and Proteins

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