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MHC I stabilizing potential of computer-designed octapeptides.

Experimental results are presented for 180 in silico designed octapeptide sequences and their stabilizing effects on the major histocompatibility class I molecule H-2K(b). Peptide sequence design was accomplished by a combination of an ant colony optimization algorithm with artificial neural network...

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Published in:Journal of Biomedicine & Biotechnology pp. 9p - 10
Main Authors: Wisniewska JM, Jäger N, Freier A, Losch FO, Wiesmüller KH, Walden P, Wrede P, Schneider G, Hiss JA
Format: research tables/charts Journal Article
Published: Wiley-Blackwell 2010
Online Access:View this record in EBSCOhost
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      dt: 2010
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      pub: Wiley-Blackwell
      place: Malden, Massachusetts
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        105082199
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        10.1155/2010/396847
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        atl: MHC I stabilizing potential of computer-designed octapeptides.
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        au:
          Wisniewska JM
          Jäger N
          Freier A
          Losch FO
          Wiesmüller KH
          Walden P
          Wrede P
          Schneider G
          Hiss JA
        affil: Institute of Organic Chemistry and Chemical Biology, Johann Wolfgang Goethe-Universität, Siesmayerstrasse. 70, 60323 Frankfurt am Main, Germany.
      sug:
        subj:
          Computers and Computerization
          Genes
          Peptides
          Algorithms
          Neural Networks (Computer)
          Proteins
      ab: Experimental results are presented for 180 in silico designed octapeptide sequences and their stabilizing effects on the major histocompatibility class I molecule H-2K(b). Peptide sequence design was accomplished by a combination of an ant colony optimization algorithm with artificial neural network classifiers. Experimental tests yielded nine H-2K(b) stabilizing and 171 nonstabilizing peptides. 28 among the nonstabilizing octapeptides contain canonical motif residues known to be favorable for MHC I stabilization. For characterization of the area covered by stabilizing and non-stabilizing octapeptides in sequence space, we visualized the distribution of 100,603 octapeptides using a self-organizing map. The experimental results present evidence that the canonical sequence motives of the SYFPEITHI database on their own are insufficient for predicting MHC I protein stabilization.
      pubtype: Academic Journal
      doctype:
        research
        tables/charts
        Journal Article
      ougenre: Article
    language: English
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