Das Shrabanti, Purkayastha Pradipta
Department of Chemical Sciences, Indian Institute of Science Education and Research (IISER) Kolkata, Mohanpur 741246, West Bengal, India.
ACS Omega. 2017 Jun 2;2(6):2451-2458. doi: 10.1021/acsomega.7b00302. eCollection 2017 Jun 30.
Harmful UVC (200-280 nm) radiation is entirely screened by a combination of dioxygen and ozone in the stratosphere. However, because of environmental pollution, depletion of stratospheric ozone layer is increasing alarmingly, ensuing danger of penetration of the harmful UVC through the earth's atmosphere to reach the living world. Studies have shown that UVC radiation accelerates aging of albumin solutions along with other qualitative changes. Herein, we have used in situ grown and ex situ added gold nanoclusters (AuNCs) to minimize the damage in the protein structure caused by long-term UVC exposure. The effects were demonstrated in the absence and presence of lipid vesicles to mimic the biological environment. Bovine serum albumin (BSA) has been used as the model protein that contains ∼50-60% helicity. It is observed that UVC converts most of α-helix into β-sheet, leading to the aggregation of protein. The ingrown AuNCs could provide about 23-40% protection to the secondary structure, whereas the externally added AuNCs preserved almost 73-82%. To generalize this finding, we have also studied the effect of AuNC protection on the UVC-exposed lysozyme protein. The results show that the proposed method is indeed helpful for life.
有害的UVC(200-280纳米)辐射完全被平流层中的氧气和臭氧的组合所屏蔽。然而,由于环境污染,平流层臭氧层的消耗正以惊人的速度增加,随之而来的危险是有害的UVC穿透地球大气层到达生物界。研究表明,UVC辐射会加速白蛋白溶液的老化以及其他质量变化。在此,我们使用原位生长和异位添加的金纳米团簇(AuNCs)来最小化长期UVC暴露对蛋白质结构造成的损害。在有无脂质体的情况下展示了这些效果,以模拟生物环境。牛血清白蛋白(BSA)被用作含有约50-60%螺旋度的模型蛋白质。观察到UVC将大部分α-螺旋转化为β-折叠,导致蛋白质聚集。原位生长的AuNCs可以为二级结构提供约23-40%的保护,而异位添加的AuNCs几乎保留了73-82%。为了推广这一发现,我们还研究了AuNC保护对UVC照射的溶菌酶蛋白的影响。结果表明,所提出的方法确实对生命有益。