Heat shock protein expression can be induced by heat shock making it possible to artificially modulate their levels noninvasively in vivo in a spatially and temporally controlled manner. Here, we report the use of the major heat shock protein 70 (HSP70) as an inducible target by using the small molecule deoxyspergualin (DSG) conjugated to the near-infrared fluorophore (Cy5.5). We demonstrate that heat induction in the form of localized hyperthermia of normal tissue in living mice results in sufficient HSP70 overexpression for detection with DSG-Cy5.5 conjugate. This effect is dependent on total energy delivered and reaches maximum fluorescence signal in 6 to 8 hours post heat induction and declines over a period of up to 24 hours. These results suggest that DSG-Cy5.5 agent accumulates in tissue with elevated HSP70 by heat.

热休克蛋白的表达可以通过热休克诱导，从而可以在体内以空间和时间受控的方式人为地调节它们的水平。在这里，我们通过使用与近红外荧光团 (Cy5.5) 结合的小分子脱氧精胍菌素 (DSG) 来报告使用主要热休克蛋白 70 (HSP70) 作为诱导靶点。我们证明了活体小鼠正常组织局部热疗形式的热诱导导致足够的 HSP70 过表达，用于检测 DSG-Cy5.5 偶联物。这种效应取决于传递的总能量，并在热诱导后 6 至 8 小时内达到最大荧光信号，并在长达 24 小时的时间内下降。这些结果表明 DSG-Cy5.5 试剂因热而在 HSP70 升高的组织中积聚。