primarily decreases during protein misfolding but viscosity mainly increases upon the formation of insoluble aggregates. We quantified the polarity of aggregated protein-of-interest in live cells via HaloTag bioorthogonal labeling, revealing polarity heterogeneity within cellular aggregates. The enriched micro-environment details inside misfolded and aggregated proteins may correlate to their bio-chemical
我们报告了一种结晶诱导的发射荧光团来定量询问聚合蛋白质的极性。这种溶剂化变色探针,即“AggRetina”探针,固有地与聚集的蛋白质结合,并表现出依赖于极性的荧光发射波长偏移和依赖于粘度的荧光强度增加。其极性敏感性的调节是通过延长共轭长度来实现的。不同的蛋白质在聚集时具有不同的极性,导致对蛋白
水解的不同抵抗力。极性主要在蛋白质错误折叠期间降低,但粘度主要在不溶性聚集体形成时增加。我们通过 HaloTag
生物正交标记量化了活细胞中聚集的目标蛋白的极性,揭示细胞聚集体内的极性异质性。错误折叠和聚集蛋白质中丰富的微环境细节可能与其生化特性和致病性相关。