Planta Med 2014; 80 - PH4
DOI: 10.1055/s-0034-1382611

Identification and study of SQAP-binding proteins from a T7 phage display screen

J Izaguirre-Carbonell 1, H Murata 1, K Ohta 1, T Kusayanagi 1, S Tsukuda 1, K Iwabata 1, Y Kanai 1, S Kamisuki 1, K Sakaguchi 1, F Sugawara 1
  • 1Department of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba 278 – 8510, Japan

Sulfoquynovosylacylpropanediol (SQAP) was chemically designed from SQMG isolated from sea urchins as a result of natural products research. SQAP performed synergistically inhibition of angiogenesis at low doses in a combination therapy with ionizing radiation. However, the radiobiological mechanisms of SQAP remain unknown. We performed a T7 phage display screen in order to identify SQAP binding proteins. We could identify five SQAP-binding proteins including Focal Adhesion Kinase (FAK). Two independent experiments were used to verify the interactions. We observed that SQAP can modulate FAK phosphorylation induced by VEGF. Additionally, downregulation of HDAC1 has been observed under SQAP treatment. Therefore, we have investigated histone acetylation level and observed an upregulated acetylation induced by SQAP.