Evaluating the potential of fluorinated tyrosines as spectroscopic probes of local protein environments: a UV resonance Raman study.
Evaluating the potential of fluorinated tyrosines as spectroscopic probes of local protein environments: a UV resonance Raman study.
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DOI：
10.1021/bi0202676
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发表时间：
2003-03
期刊：
影响因子：
2.9
通讯作者：
P. Reid;C. Loftus;C. Beeson
中科院分区：
文献类型：
--
作者：
P. Reid;C. Loftus;C. Beeson
介绍了用紫外共振拉曼(UVRR)研究氟化酪氨酸作为当地环境光谱探针的可行性。特别报道了2-氟-L-酪氨酸和3-氟-L-酪氨酸(3-Y(F))在229 nm激发下的共振拉曼光谱。与酪氨酸共振拉曼光谱对环境的适度依赖不同，3-Y(F)的光谱被发现与周围环境的氢键强度密切相关。初步从头算研究表明，这种行为是由于C-OH和C-F内部坐标对正常模式的主要贡献。氢键与溶剂的结合扰乱了内部配位能级和/或耦合，从而改变了简正模的性质以及相应的跃迁频率和/或强度。除了溶剂研究外，3-Y(F)还被特异性地结合到流感血凝素(HA)100-107肽中，它与17/9抗HA(98-108)多肽抗体的Fv片段结合。这些研究表明，在天然酪氨酸存在的情况下，可以监测3-Y(F)的光谱。综上所述，这里提出的研究表明，3-Y(F)作为蛋白质环境的探测器具有特殊的前景。
Ultraviolet resonance Raman (UVRR) studies designed to test the utility of fluorinated tyrosines as spectroscopic probes of the local environment are presented. Specifically, resonance Raman spectra of 2-fluoro-L-tyrosine and 3-fluoro-L-tyrosine (3-Y(f)) obtained with 229 nm excitation are reported. In contrast to the modest environmental dependence of the tyrosine resonance Raman spectrum, the spectrum of 3-Y(f) is found to be extremely dependent on the hydrogen bonding strength of the surrounding environment. Preliminary ab initio studies suggest that this behavior is due to normal modes having dominant contributions from the C-OH and C-F internal coordinates. Hydrogen bonding to the solvent perturbs the internal coordinate energetics and/or couplings, thereby altering the character of the normal modes and the corresponding transition frequencies and/or intensities. In addition to the solvent studies, 3-Y(f) is site specifically incorporated into the influenza hemagglutinin (HA) 100-107 peptide which binds to the Fv fragment of the 17/9 anti-HA(98-108) peptide antibody. These studies demonstrate that the spectrum of 3-Y(f) can be monitored in the presence of native tyrosine. In summary, the studies presented here demonstrate that 3-Y(f) holds exceptional promise as a probe of the protein environment.