An FPGA Implementation to Detect Selective Cationic Antibacterial Peptides
Author(s) -
Carlos Polanco,
Marco Aurelio NuñoMaganda,
Miguel Arias-Estrada,
Gabriel del Rio
Publication year - 2011
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0021399
Subject(s) - field programmable gate array , computer science , scalability , gate array , antibacterial peptide , identification (biology) , cationic polymerization , code (set theory) , sequence (biology) , peptide , embedded system , parallel computing , antibacterial activity , combinatorial chemistry , computer architecture , chemistry , biology , biochemistry , bacteria , database , organic chemistry , botany , genetics , set (abstract data type) , programming language
Exhaustive prediction of physicochemical properties of peptide sequences is used in different areas of biological research. One example is the identification of selective cationic antibacterial peptides (SCAPs), which may be used in the treatment of different diseases. Due to the discrete nature of peptide sequences, the physicochemical properties calculation is considered a high-performance computing problem. A competitive solution for this class of problems is to embed algorithms into dedicated hardware. In the present work we present the adaptation, design and implementation of an algorithm for SCAPs prediction into a Field Programmable Gate Array (FPGA) platform. Four physicochemical properties codes useful in the identification of peptide sequences with potential selective antibacterial activity were implemented into an FPGA board. The speed-up gained in a single-copy implementation was up to 108 times compared with a single Intel processor cycle for cycle. The inherent scalability of our design allows for replication of this code into multiple FPGA cards and consequently improvements in speed are possible. Our results show the first embedded SCAPs prediction solution described and constitutes the grounds to efficiently perform the exhaustive analysis of the sequence-physicochemical properties relationship of peptides.
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