Schütt Markus, Krupka Simone S, Milbradt Alexander G, Deindl Sebastian, Sinner Eva Kathrin, Oesterhelt Dieter, Renner Christian, Moroder Luis
Max-Planck-Institut für Biochemie, Am Klopferspitz 18A, 82152, Martinsried, Germany.
Chem Biol. 2003 Jun;10(6):487-90. doi: 10.1016/s1074-5521(03)00128-5.
A photoresponsive integrin ligand was synthesized by backbone-cyclization of a heptapeptide containing the integrin binding motif Arg-Gly-Asp (RGD) with 4-(aminomethyl)phenylazobenzoic acid (AMPB). Surface plasmon enhanced fluorescence spectroscopy showed that binding of the azobenzene peptide to alpha(v)beta(3) integrin depends on the photoisomeric state of the peptide chromophore. The higher affinity of the trans isomer could be rationalized by comparing the NMR conformations of the cis and trans isomers with the recently solved X-ray structure of a cyclic RGD-pentapeptide bound to integrin.
通过将含有整合素结合基序精氨酸-甘氨酸-天冬氨酸（RGD）的七肽与4-（氨甲基）苯基偶氮苯甲酸（AMPB）进行主链环化反应，合成了一种光响应性整合素配体。表面等离子体增强荧光光谱表明，偶氮苯肽与α(v)β(3)整合素的结合取决于肽发色团的光异构状态。通过比较顺式和反式异构体的核磁共振构象与最近解析的与整合素结合的环状RGD-五肽的X射线结构，可以解释反式异构体具有更高的亲和力。
