NILE RED AS A POLARITY-SENSITIVE FLUORESCENT-PROBE OF HYDROPHOBIC PROTEIN SURFACES
NILE RED AS A POLARITY-SENSITIVE FLUORESCENT-PROBE OF HYDROPHOBIC PROTEIN SURFACES
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DOI：
10.1016/0003-2697(87)90157-6
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发表时间：
1987-12-01
影响因子：
2.9
通讯作者：
WOLFF, J
中科院分区：
文献类型：
--
作者：
SACKETT, DL;WOLFF, J
尼罗红是一种不带电荷的疏水分子，其荧光受到其环境极性的强烈影响。它与许多但不是所有的天然蛋白质相互作用，包括β-乳球蛋白，κ-酪蛋白和白蛋白，对于不同的蛋白质具有宽范围的光谱变化。它检测暴露或形成新的疏水表面诱导配体结合钙调蛋白，蜂毒肽寡聚化，或展开卵清蛋白在早期热变性。该染料是光稳定的，工作波长范围宽，并且从许多生物分子吸收的波长范围中去除，荧光不受pH 4.5和8.5之间的影响，量子产率高，并且可以在稀溶液中研究蛋白质上的疏水位点。
Nile red is an uncharged hydrophobic molecule whose fluorescence is strongly influenced by the polarity of its environment. It interacts with many, but not all, native proteins, including .beta.-lactoglobulin, .kappa.-casein, and albumin, with a wide range of spectral changes for different proteins. It detects the exposure or formation of new hydrophobic surfaces induced by ligand binding to calmodulin, oligomerization of melittin, or unfolding of ovalbumin during early thermal denaturation. The dye is photostable, the working wavelength range is broad and removed from those at which many biomolecules absorb, the fluorescence is unaffected by pH between 4.5 and 8.5, the quantum yield is high, and hydrophobic site on proteins may be investigated in dilute solutions.