Kauer J C, Erickson-Viitanen S, Wolfe H R, DeGrado W F
J Biol Chem. 1986 Aug 15;261(23):10695-700.
A new photoreactive amino acid analog, p-benzoyl-L-phenylalanine, is described. Convenient methods for the preparation of this amino acid and its subsequent incorporation into synthetic peptides by the solid-phase technique are outlined. To illustrate its utility, p-benzoyl-L-phenylalanine was substituted in place of tryptophan in a 17-residue calmodulin-binding peptide. The substitution did not measurably affect the affinity of this peptide for calmodulin. When this peptide was photolyzed at 350 nm in a 1:1 molar ratio with calmodulin in the presence of 500 microM CaCl2, 70% of the calmodulin was derivatized. The specificity of the reaction was investigated by photolysis in the absence of CaCl2 where little binding occurs; under these conditions little or no photolabeling occurred.
描述了一种新的光反应性氨基酸类似物，对苯甲酰基-L-苯丙氨酸。概述了制备该氨基酸及其随后通过固相技术掺入合成肽的简便方法。为说明其效用，在一个17个残基的钙调蛋白结合肽中，用对苯甲酰基-L-苯丙氨酸取代色氨酸。该取代对该肽与钙调蛋白的亲和力没有明显影响。当该肽在500 microM氯化钙存在下与钙调蛋白以1:1摩尔比在350 nm处光解时，70%的钙调蛋白被衍生化。通过在几乎不发生结合的无氯化钙条件下进行光解来研究反应的特异性；在这些条件下几乎没有或没有发生光标记。
