RT Journal Article
SR Electronic
T1 PIPI: PTM-Invariant Peptide Identification Using Coding Method
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 055806
DO 10.1101/055806
A1 Fengchao Yu
A1 Ning Li
A1 Weichuan Yu
YR 2016
UL http://biorxiv.org/content/early/2016/05/27/055806.abstract
AB In computational proteomics, identification of peptides with an unlimited number of post-translational modification (PTM) types is a challenging task. The computational cost increases exponentially with respect to the number of modifiable amino acids and linearly with respect to the number of potential PTM types at each amino acid. The problem becomes intractable very quickly if we want to enumerate all possible modification patterns. Existing tools (e.g., MS-Alignment, ProteinProspector, and MODa) avoid enumerating modification patterns in database search by using an alignment-based approach to localize and characterize modified amino acids. This approach avoids enumerating all possible modification patterns in a database search. However, due to the large search space and PTM localization issue, the sensitivity of these tools is low. This paper proposes a novel method named PIPI to achieve PTM-invariant peptide identification. PIPI first codes peptide sequences into Boolean vectors and converts experimental spectra into real-valued vectors. Then, it finds the top 10 peptide-coded vectors for each spectrum-coded vector. After that, PIPI uses a dynamic programming algorithm to localize and characterize modified amino acids. Simulations and real data experiments have shown that PIPI outperforms existing tools by identifying more peptide-spectrum matches (PSMs) and reporting fewer false positives. It also runs much faster than existing tools when the database is large.