Molecular design of LPS-binding peptides

作者：Suzuki Masatsugu Matt; Matsumoto Megumi; Yamamoto Akihiko; Ochiai Masaki; Horiuchi Yoshinobu; Niwa Makoto; Omi Hiroyuki; Kobayashi Tomomi; Takagi Takashi^*

来源：Journal of Microbiological Methods, 2010, 83(2): 153-155.

DOI：10.1016/j.mimet.2010.08.009

• LPS-binding peptides
• Phage display
• Li5-025
• Li5-001

Lipopolysaccharide (LPS), a major constituent of the outer membrane of Gram-negative bacteria, is highly toxic and can cause sepsis or septic shock. Therefore, detection of LPS and the ability to neutralize its toxicity is important. We previously obtained a strong LPS-binding peptide, Li5-001, using the phage display method (Matsumoto et al., 2010. J. Microbiol. Methods. 82, 54-58). We modified the sequence the amino acid sequence of this peptide (KNYSSSISSIHAC), by replacing and deleting amino acids to obtain higher LPS-binding affinity and greater resistance to protease digestion. Consequently we obtained a dodecapeptide, Li5-025 (K'YSSSISSIRAC', K' and C' are D-forms of K and C. respectively) which showed a high affinity for LPS, approximately 1000 folds higher affinity than Li5-001 and Kd value of 0.01 nM. By replacing both N- and C-terminal amino acids from L-type to D-type, the peptide was rendered resistant to protease digestion without altering its overall binding capacity.

• 出版日期2010-11