A fluorescence study of the binding of calcium and terbium ions to angiotensin

Robert E. Lenkinski , Jerry D. Glickson , Roderich Walter
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引用次数: 11

Abstract

The interactions of angiotensin II and a synthetic analogue, [Asn1, Val5] angiotensin II, with Ca2+ and Tb3+ have been monitored using the intrinsic fluorescence of the tyrosine residue at position 4 in both molecules. The data indicate that angiotensin II binds both metals with a dissociation constant of ∼1 × 10−4 M−1, while no significant binding was observed with the amide analogue. This suggests that the side chain carboxyl group of aspartic acid forms part of the binding site. Since the value of the dissociation constant suggests chelation of the metals by the hormone, the terminal carboxyl group of the peptide is also probably involved in metal binding. The fact that energy transfer was observed between Tb3+ and the tyrosine of angiotensin places the hydroxl or carbonyl group of the tyrosine close to the metal binding site.

钙和铽离子与血管紧张素结合的荧光研究
血管紧张素II及其合成类似物[Asn1, Val5]血管紧张素II与Ca2+和Tb3+的相互作用已被监测,利用这两种分子中4位酪氨酸残基的固有荧光。数据表明,血管紧张素II与这两种金属结合的解离常数为~ 1 × 10−4 M−1,而与酰胺类似物没有明显的结合。这表明天冬氨酸的侧链羧基构成了结合位点的一部分。由于解离常数的值表明激素对金属的螯合作用,肽的末端羧基也可能参与金属结合。在Tb3+和血管紧张素的酪氨酸之间观察到的能量转移使酪氨酸的羟基或羰基靠近金属结合位点。
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