New method of peptide cleavage based on Edman degradation

Bąchor, Remigiusz; Kluczyk, Alicja; Stefanowicz, Piotr; Szewczuk, Zbigniew

doi:10.1007/s11030-013-9453-y

Cited by 18 publications

(11 citation statements)

References 27 publications

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“…Madru et al [ 40 ] covalently immobilized anticocaine aptamer conjugated amine on CNBr-activated sepharose. However, there is growing concern associated with high toxicity of CNBr and its potentiality as an environmental pollutant [ 41 ]. In addition, surface immobilization of CNBr is time consuming, which may inactivate the biological activity of aptamer.…”

Section: Functionalization Of Aptamers For Biodecontaminationmentioning

confidence: 99%

Aptamers as the Agent in Decontamination Assays (Apta-Decontamination Assays): From the Environment to the Potential Application In Vivo

Bilibana

Citartan

Yeoh

et al. 2017

Journal of Nucleic Acids

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The binding specificity and affinity of aptamers have long been harnessed as the key elements in the development of aptamer-based assays, particularly aptasensing application. One promising avenue that is currently explored based on the specificity and affinity of aptamers is the application of aptamers in the decontamination assays. Aptamers have been successfully harnessed as the decontamination agents to remove contaminants from the environment and to decontaminate infectious elements. The reversible denaturation property inherent in aptamers enables the repeated usage of aptamers, which can immensely save the cost of decontamination. Analogous to the point-of-care diagnostics, there is no doubt that aptamers can also be deployed in the point-of-care aptamer-based decontamination assay, whereby decontamination can be performed anywhere and anytime for instantaneous decision-making. It is also prophesied that aptamers can also serve more than as a decontaminant, probably as a tool to capture and kill hazardous elements, particularly pathogenic agents.

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Section: Functionalization Of Aptamers For Biodecontaminationmentioning

confidence: 99%

Aptamers as the Agent in Decontamination Assays (Apta-Decontamination Assays): From the Environment to the Potential Application In Vivo

Bilibana

Citartan

Yeoh

et al. 2017

Journal of Nucleic Acids

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“…This was done, as although the sequence may have some protein level evidence, identifying these proteins experimentally using shotgun proteomics would not be possible. "X" denotes ambiguous amino acids in protein sequences; they arise due to either the presence of multiple sequences showing different amino acids, or poor quality data that is unable to distinguish between amino acids (53,54).…”

Section: Database Constructionmentioning

confidence: 99%

Mapping Coeliac Toxic Motifs in the Prolamin Seed Storage Proteins of Barley, Rye, and Oats Using a Curated Sequence Database

et al. 2020

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Wheat gluten, and related prolamin proteins in rye, barley and oats cause the immune-mediated gluten intolerance syndrome, coeliac disease. Foods labelled as gluten-free which can be safely consumed by coeliac patients, must not contain gluten above a level of 20 mg/Kg. Current immunoassay methods for detection of gluten can give conflicting results and may underestimate levels of gluten in foods. Mass spectrometry methods have great potential as an orthogonal method, but require curated protein sequence databases to support method development. The GluPro database has been updated to include avenin-like sequences from bread wheat (n = 685; GluPro v1.1) and genes from the sequenced wheat genome (n = 699; GluPro v 1.2) and Triticum turgidum ssp durum (n = 210; GluPro v 2.1). Companion databases have been developed for prolamin sequences from barley (n = 64; GluPro v 3.0), rye (n = 41; GluPro v 4.0), and oats (n = 27; GluPro v 5.0) and combined to provide a complete cereal prolamin database, GluPro v 6.1 comprising 1,041 sequences. Analysis of the coeliac toxic motifs in the curated sequences showed that they were absent from the minor avenin-like proteins in bread and durum wheat and barley, unlike the related avenin proteins from oats. A comparison of prolamin proteins from the different cereal species also showed α-and γ-gliadins in bread and durum wheat, and the sulphur poor prolamins in all cereals had the highest density of coeliac toxic motifs. Analysis of ion-mobility mass spectrometry data for bread wheat (cvs Chinese Spring and Hereward) showed an increased number of identifications when using the GluPro v1.0, 1.1 and 1.2 databases compared to the limited number of verified sequences bread wheat sequences in reviewed UniProt. This family of databases will provide a basis for proteomic profiling of gluten proteins from all the gluten containing cereals and support identification of specific peptide markers for use in development of new methods for gluten quantitation based on coeliac toxic motifs found in all relevant cereal species.

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“…In addition, peptides derivatized with N , N , N ‐trialkylglycine residue are susceptible to base‐catalyzed hydrogen‐ deuterium exchange at the α‐carbon atom. This reaction dramatically slows down at a lower pH, therefore incorporated deuterons are stable during LC‐MS analysis and may be utilized in the quantification of peptides by the isotopic dilution method (Bąchor et al, ; Bąchor et al, ; Bąchor et al, ; Cydzik et al, ; Cydzik et al, ; Rudowska et al, ; Rudowska et al, ).…”

Section: Ms Research In Polandmentioning

confidence: 99%

Mass spectrometry for the elucidation of the subtle molecular structure of biodegradable polymers and their degradation products

Kowalczuk

Adamus

2015

Mass Spectrometry Reviews

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Contemporary reports by Polish authors on the application of mass spectrometric methods for the elucidation of the subtle molecular structure of biodegradable polymers and their degradation products will be presented. Special emphasis will be given to natural aliphatic (co)polyesters (PHA) and their synthetic analogues, formed through anionic ring-opening polymerization (ROP) of b-substituted b-lactones. Moreover, the application of MS techniques for the evaluation of the structure of biodegradable polymers obtained in ionic and coordination polymerization of cyclic ethers and esters as well as products of step-growth polymerization, in which bifunctional or multifunctional monomers react to form oligomers and eventually long chain polymers, will be discussed. Furthermore, the application of modern MS techniques for the assessment of polymer degradation products, frequently bearing characteristic end groups that can be revealed and differentiated by MS, will be discussed within the context of specific degradation pathways. Finally, recent Polish accomplishments in the area of mass spectrometry will be outlined. # 2015 Wiley Periodicals, Inc. Mass Spec Rev 35: 188-198, 2016.

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New method of peptide cleavage based on Edman degradation

Cited by 18 publications

References 27 publications

Aptamers as the Agent in Decontamination Assays (Apta-Decontamination Assays): From the Environment to the Potential Application In Vivo

Aptamers as the Agent in Decontamination Assays (Apta-Decontamination Assays): From the Environment to the Potential Application In Vivo

Mapping Coeliac Toxic Motifs in the Prolamin Seed Storage Proteins of Barley, Rye, and Oats Using a Curated Sequence Database

Mass spectrometry for the elucidation of the subtle molecular structure of biodegradable polymers and their degradation products

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