Prediction of peptide drift time in ion mobility mass spectrometry from sequence-based features
Online Publication Date2013-05-09
Print Publication Date2013
Permanent link to this recordhttp://hdl.handle.net/10754/325237
MetadataShow full item record
AbstractBackground: Ion mobility-mass spectrometry (IMMS), an analytical technique which combines the features of ion mobility spectrometry (IMS) and mass spectrometry (MS), can rapidly separates ions on a millisecond time-scale. IMMS becomes a powerful tool to analyzing complex mixtures, especially for the analysis of peptides in proteomics. The high-throughput nature of this technique provides a challenge for the identification of peptides in complex biological samples. As an important parameter, peptide drift time can be used for enhancing downstream data analysis in IMMS-based proteomics.Results: In this paper, a model is presented based on least square support vectors regression (LS-SVR) method to predict peptide ion drift time in IMMS from the sequence-based features of peptide. Four descriptors were extracted from peptide sequence to represent peptide ions by a 34-component vector. The parameters of LS-SVR were selected by a grid searching strategy, and a 10-fold cross-validation approach was employed for the model training and testing. Our proposed method was tested on three datasets with different charge states. The high prediction performance achieve demonstrate the effectiveness and efficiency of the prediction model.Conclusions: Our proposed LS-SVR model can predict peptide drift time from sequence information in relative high prediction accuracy by a test on a dataset of 595 peptides. This work can enhance the confidence of protein identification by combining with current protein searching techniques. 2013 Wang et al.; licensee BioMed Central Ltd.
CitationWang B, Zhang J, Chen P, Ji Z, Deng S, et al. (2013) Prediction of peptide drift time in ion mobility mass spectrometry from sequence-based features. BMC Bioinformatics 14: S9. doi:10.1186/1471-2105-14-S8-S9.
PubMed Central IDPMC3654891
The following license files are associated with this item:
Except where otherwise noted, this item's license is described as This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
- Artificial neural networks for the prediction of peptide drift time in ion mobility mass spectrometry.
- Authors: Wang B, Valentine S, Plasencia M, Raghuraman S, Zhang X
- Issue date: 2010 Apr 11
- Prediction of drift time in ion mobility-mass spectrometry based on Peptide molecular weight.
- Authors: Wang B, Valentine S, Plasencia M, Zhang X
- Issue date: 2010 Sep
- [A new peptide retention time prediction method for mass spectrometry based proteomic analysis by a serial and parallel support vector machine model].
- Authors: Zhang J, Zhang D, Zhang W, Xie H
- Issue date: 2012 Sep
- Machine learning based prediction for peptide drift times in ion mobility spectrometry.
- Authors: Shah AR, Agarwal K, Baker ES, Singhal M, Mayampurath AM, Ibrahim YM, Kangas LJ, Monroe ME, Zhao R, Belov ME, Anderson GA, Smith RD
- Issue date: 2010 Jul 1
- Modeling and prediction of peptide drift times in ion mobility spectrometry using sequence-based and structure-based approaches.
- Authors: Zhang Y, Jin Q, Wang S, Ren R
- Issue date: 2011 May
Showing items related by title, author, creator and subject.
Phosphoproteome analysis during larval development and metamorphosis in the spionid polychaete Pseudopolydora vexillosaChandramouli, Kondethimmanahalli; Mok, Flora SY; Wang, Hao; Qian, Pei-Yuan (BMC Developmental Biology, Springer Nature, 2011-06-24) [Article]Background: The metamorphosis of the spionid polychaete Pseudopolydora vexillosa includes spontaneous settlement onto soft-bottom habitats and morphogenesis that can be completed in a very short time. A previous study on the total changes to the proteome during the various developmental stages of P. vexillosa suggested that little or no de novo protein synthesis occurs during metamorphosis. In this study, we used multicolor fluorescence detection of proteins in 2-D gels for differential analysis of proteins and phosphoproteins to reveal the dynamics of post-translational modification proteins in this species. A combination of affinity chromatography, 2D-PAGE, and mass spectrometry was used to identify the phosphoproteins in pre-competent larvae, competent larvae, and newly metamorphosed juveniles. Results: We reproducibly detected 210, 492, and 172 phosphoproteins in pre-competent larvae, competent larvae, and newly metamorphosed juveniles, respectively. The highest percentage of phosphorylation was observed during the competent larval stage. About 64 stage-specific phosphoprotein spots were detected in the competent stage, and 32 phosphoproteins were found to be significantly differentially expressed in the three stages. We identified 38 phosphoproteins, 10 of which were differentially expressed during metamorphosis. These phosphoproteins belonged to six categories of biological processes: (1) development, (2) cell differentiation and integrity, (3) transcription and translation, (4) metabolism, (5) protein-protein interaction and proteolysis, and (6) receptors and enzymes. Conclusion: This is the first study to report changes in phosphoprotein expression patterns during the metamorphosis of the marine polychaete P. vexillosa. The higher degree of phosphorylation during the process of attaining competence to settle and metamorphose may be due to fast morphological transitions regulated by various mechanisms. Our data are consistent with previous studies showing a high percentage of phosphorylation during competency in the barnacle Balanus amphitrite and the bryozoan Bugula neritina. The identified phosphoproteins may play an important role during metamorphosis, and further studies on the location and functions of important proteins during metamorphosis are warranted. © 2011 Chandramouli et al; licensee BioMed Central Ltd.
Analysis of plasma protein adsorption onto DC-Chol-DOPE cationic liposomes by HPLC-CHIP coupled to a Q-TOF mass spectrometerCapriotti, Anna Laura; Caracciolo, Giulio; Caruso, Giuseppe; Cavaliere, Chiara; Pozzi, Daniela; Samperi, Roberto; Laganà, Aldo (Analytical and Bioanalytical Chemistry, Springer Nature, 2010-09-22) [Article]Plasma protein adsorption is regarded as a key factor in the in vivo organ distribution of intravenously administered drug carriers, and strongly depends on vector surface characteristics. The present study aimed to characterize the "protein corona" absorbed onto DC-Chol-DOPE cationic liposomes. This system was chosen because it is one of the most efficient and widely used non-viral formulations in vitro and a potential candidate for in vivo transfection of genetic material. After incubation of human plasma with cationic liposomes, nanoparticle-protein complex was separated from plasma by centrifugation. An integrated approach based on protein separation by one-dimensional 12% polyacrylamide gel electrophoresis followed by the automated HPLC-Chip technology coupled to a high-resolution mass spectrometer was employed for protein corona characterization. Thirty gel lanes, approximately 2 mm, were cut, digested and analyzed by HPLC-MS/MS. Fifty-eight human plasma proteins adsorbed onto DC-Chol-DOPE cationic liposomes were identified. The knowledge of the interactions of proteins with liposomes can be exploited for future controlled design of colloidal drug carriers and possibly in the controlled creation of biocompatible surfaces of other devices that come into contact with proteins in body fluids. © 2010 Springer-Verlag.
Proteomic analysis during larval development and metamorphosis of the spionid polychaete Pseudopolydora vexillosaMok, Flora SY; Thiyagarajan, Vengatesen; Qian, Pei-Yuan (Proteome Science, Springer Nature, 2009-12-17) [Article]Background: While the larval-juvenile transition (metamorphosis) in the spionid polychaete Pseudopolydora vexillosa involves gradual morphological changes and does not require substantial development of juvenile organs, the opposite occurs in the barnacle Balanus amphitrite. We hypothesized that the proteome changes during metamorphosis in the spionids are less drastic than that in the barnacles. To test this, proteomes of pre-competent larvae, competent larvae (ready to metamorphose), and juveniles of P. vexillosa were compared using 2-dimensional gel electrophoresis (2-DE), and they were then compared to those of the barnacle.Results: Unlike the significant changes found during barnacle metamorphosis, proteomes of competent P. vexillosa larvae were more similar to those of their juveniles. Pre-competent larvae had significantly fewer protein spots (384 spots), while both competent larvae and juveniles expressed about 660 protein spots each. Proteins up-regulated during competence identified by MALDI-TOF/TOF analysis included a molecular chaperon (calreticulin), a signal transduction regulator (tyrosin activation protein), and a tissue-remodeling enzyme (metallopeptidase).Conclusions: This was the first time to study the protein expression patterns during the metamorphosis of a marine polychaete and to compare the proteomes of marine invertebrates that have different levels of morphological changes during metamorphosis. The findings provide promising initial steps towards the development of a proteome database for marine invertebrate metamorphosis, thus deciphering the possible mechanisms underlying larval metamorphosis in non-model marine organisms. © 2009 Mok et al; licensee BioMed Central Ltd.