論文

査読有り 国際誌
2015年3月

Highly stable, fluorescence-labeled heptapeptides substituted with a D-amino acid for the specific detection of oxidized low-density lipoprotein in plasma.

Chemical biology & drug design
  • Akira Sato
  • ,
  • Hikaru Yamanaka
  • ,
  • Keitaro Oe
  • ,
  • Izumi Yokoyama
  • ,
  • Yoji Yamazaki
  • ,
  • Keiichi Ebina

85
3
開始ページ
348
終了ページ
55
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1111/cbdd.12399

Probes that can detect oxidized low-density lipoprotein (ox-LDL) in plasma and in atherosclerotic plaques can be useful for the diagnosis, prevention, and treatment of atherosclerosis. Recently, we have reported that two heptapeptides (Lys-Trp-Tyr-Lys-Asp-Gly-Asp, KP6) coupled to fluorescein isothiocyanate (FITC) through the ε-amino group of N-terminus Lys in the absence/presence of 6-amino-n-caproic acid (AC) linker to FITC-(FITC)KP6 and (FITC-AC)KP6-can be useful as fluorescent probes for the specific detection of ox-LDL. In this study, to develop the fluorescent peptides with high plasma stability for the specific detection of ox-LDL, we investigated the interaction of (FITC)KP6 and (FITC-AC)KP6 substituted with D-Lys at the N-terminus-(FITC)dKP6 and (FITC-AC)dKP6-with ox-LDL, and the in vitro stability of these peptides in mouse plasma. (FITC)dKP6 and (FITC-AC)dKP6 bound with high specificity to ox-LDL in a dose-dependent manner, and also to ox-LDL in the mouse plasma. Furthermore, (FITC)dKP6 was more stable than (FITC)KP6 in mouse plasma (102.1% versus 69.0% remained after 1 h). These findings strongly suggest that (FITC)dKP6 and (FITC-AC)dKP6 may be effective fluorescent probes with higher plasma stability than (FITC)KP6 and (FITC-AC)KP6 for the specific detection of ox-LDL.

リンク情報
DOI
https://doi.org/10.1111/cbdd.12399
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/25066364
ID情報
  • DOI : 10.1111/cbdd.12399
  • PubMed ID : 25066364

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