A quantitative strategy of ultrasound-assisted digestion combined UPLC-MS/MS for rapid identifying species-specific peptide markers in the application of food gelatin authentication

ABSTRACT Currently available detectors for spores of Bacillus anthracis, the causative agent of anthrax, are inadequate for frontline use and general monitoring. There is a critical need for simple, rugged, and inexpensive detectors capable of accurate and direct identification of B. anthracis spores. Necessary components in such detectors are stable ligands that bind tightly and specifically to target spores. By screening a phage display peptide library, we identified a family of peptides, with the consensus sequence TYPXPXR, that bind selectively to B. anthracis spores. We extended this work by identifying a peptide variant, ATYPLPIR, with enhanced ability to bind to B. anthracis spores and an additional peptide, SLLPGLP, that preferentially binds to spores of species phylogenetically similar to, but distinct from, B. anthracis. These two peptides were used in tandem in simple assays to rapidly and unambiguously identify B. anthracis spores. We envision that these peptides can be used as sensors in economical and portable B. anthracis spore detectors that are essentially free of false-positive signals due to other environmental Bacillus spores.

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Genome to Kinome: Species-Specific Peptide Arrays for Kinome Analysis

Science Signaling ◽

10.1126/scisignal.254pl1 ◽

2009 ◽

Vol 2 (54) ◽

pp. pl1-pl1 ◽

Cited By ~ 59

Author(s):

S. Jalal ◽

R. Arsenault ◽

A. A. Potter ◽

L. A. Babiuk ◽

P. J. Griebel ◽

...

Keyword(s):

Peptide Arrays ◽

Species Specific ◽

Specific Peptide

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Identification of species-specific peptide markers in cold-pressed oils

Scientific Reports ◽

10.1038/s41598-020-76944-z ◽

2020 ◽

Vol 10 (1) ◽

Author(s):

Klaudia Kotecka-Majchrzak ◽

Agata Sumara ◽

Emilia Fornal ◽

Magdalena Montowska

Keyword(s):

Storage Proteins ◽

Seed Storage ◽

High Sensitivity ◽

Seed Storage Proteins ◽

Global Market ◽

Evening Primrose ◽

Allergenic Proteins ◽

Species Specific ◽

Cold Pressed ◽

Specific Peptide

AbstractIn recent years, cold-pressed vegetable oils have become very popular on the global market. Therefore, new versatile methods with high sensitivity and specificity are needed to find and combat fraudulent practices. The objective of this study was to identify oilseed species-specific peptide markers, using proteomic techniques, for authentication of 10 cold-pressed oils. In total, over 380 proteins and 1050 peptides were detected in the samples. Among those peptides, 92 were found to be species-specific and unique to coconut, evening primrose, flax, hemp, milk thistle, nigella, pumpkin, rapeseed, sesame, and sunflower oilseed species. Most of the specific peptides were released from major seed storage proteins (11 globulins, 2S albumins), and oleosins. Additionally, the presence of allergenic proteins in the cold-pressed oils, including pumpkin Cuc ma 5, sunflower Hel a 3, and six sesame allergens (Ses i 1, Ses i 2, Ses i 3, Ses i 4, Ses i 6, and Ses i 7) was confirmed in this study. This study provides novel information on specific peptides that will help to monitor and verify the declared composition of cold-pressed oil as well as the presence of food allergens. This study can be useful in the era of widely used unlawful practices.

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A predictive model for vertebrate bone identification from collagen using proteomic mass spectrometry

Scientific Reports ◽

10.1038/s41598-021-90231-5 ◽

2021 ◽

Vol 11 (1) ◽

Author(s):

Heyi Yang ◽

Erin R. Butler ◽

Samantha A. Monier ◽

Jennifer Teubl ◽

David Fenyö ◽

...

Keyword(s):

Mass Spectrometry ◽

Species Identification ◽

Probabilistic Approach ◽

Modern Human ◽

Peptide Sequence ◽

Human Species ◽

Interpretation Errors ◽

Species Specific ◽

Sequence Errors ◽

Specific Peptide

AbstractProteogenomics is an increasingly common method for species identification as it allows for rapid and inexpensive interrogation of an unknown organism’s proteome—even when the proteome is partially degraded. The proteomic method typically uses tandem mass spectrometry to survey all peptides detectable in a sample that frequently contains hundreds or thousands of proteins. Species identification is based on detection of a small numbers of species-specific peptides. Genetic analysis of proteins by mass spectrometry, however, is a developing field, and the bone proteome, typically consisting of only two proteins, pushes the limits of this technology. Nearly 20% of highly confident spectra from modern human bone samples identify non-human species when searched against a vertebrate database—as would be necessary with a fragment of unknown bone. These non-human peptides are often the result of current limitations in mass spectrometry or algorithm interpretation errors. Consequently, it is difficult to know if a “species-specific” peptide used to identify a sample is actually present in that sample. Here we evaluate the causes of peptide sequence errors and propose an unbiased, probabilistic approach to determine the likelihood that a species is correctly identified from bone without relying on species-specific peptides.

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