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MALDI-TOF Analysis of Binding between DNA and Peptides Containing Lysine and Tryptophan

Lee, Seonghyun;Choe, Sojeong;Oh, Yeeun;Jo, Kyubong

  • Received : 2015.08.25
  • Accepted : 2015.09.15
  • Published : 2015.09.30

Abstract

Here, we demonstrate the use of MALDI-TOF as a fast and simple analytical approach to evaluate the DNA-binding capability of various peptides. Specifically, by varying the amino acid sequence of the peptides consisting of lysine (K) and tryptophan (W), we identified peptides with strong DNA-binding capabilities using MALDI-TOF. Mass spectrometric analysis reveals an interesting novel finding that lysine residues show sequence selective preference, which used to be considered as mediator of electrostatic interactions with DNA phosphate backbones. Moreover, tryptophan residues show higher affinity to DNA than lysine residues. Since there are numerous possible combinations to make peptide oligomers, it is valuable to introduce a simple and reliable analytical approach in order to quickly identify DNA-binding peptides.

Keywords

MALDI-TOF;DNA Binding Peptide;Lysine and Tryptophan-containing Peptide;Non-covalent DNA-Peptide Binding

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