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首页> 外文会议>Biophysics, Biology, and Biophotonics: the Crossroads >Fluorescence Based Assessment of SDS Induced Hydrophobic Collapse in Globular Proteins
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Fluorescence Based Assessment of SDS Induced Hydrophobic Collapse in Globular Proteins

机译：基于荧光的SDS诱导的球状蛋白疏水性塌陷的评估

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摘要

The molecular mechanism of interaction between SDS and proteins is not clearly understood so far. According to the current knowledge SDS is known to interact with the hydrophobic regions of the proteins. Tryptophan and tyrosine are hydrophobic and hydrophilic aromatic amino acids respectively, which are also known for their intrinsic fluorescence nature in proteins. By observing the autofluorescence of both these hydrophobic and hydrophilic amino acids upon SDS treatment, information about SDS-protein interactions could be obtained. In the present study we have recorded the autofluorescence spectra of five globular proteins [Bovine serum albumin (BSA), Human serum albumin (HSA), Ribonuclease A (RNase A), Lysozyme and Trypsin] by the sequential excitation from 260nm to 295nm at every 5nm intervals. The results obtained clearly indicated BSA and HSA undergone hydrophobic collapse around their tryptophan moieties due to the increased folding of their secondary and tertiary structures upon SDS treatment. Trypsin on the other hand showed complete unfolding upon treatment with SDS. Lysozyme and RNase A did not show any difference in their autofluorescence upon SDS treatment may be due to the stability and fluorophores composition in them. The above results obtained with specific UV excitations clearly shown the tertiary folding and ensembles of the secondary and tertiary structures upon SDS treatment is governed by their stability and bonds stabilizing the proteins.
机译：到目前为止，尚不清楚SDS与蛋白质之间相互作用的分子机制。根据目前的知识，已知SDS与蛋白质的疏水区域相互作用。色氨酸和酪氨酸分别是疏水性和亲水性芳香族氨基酸，它们在蛋白质中的固有荧光性质也众所周知。通过观察SDS处理后这些疏水性氨基酸和亲水性氨基酸的自发荧光，可以获得有关SDS-蛋白质相互作用的信息。在本研究中，我们通过从260nm到295nm的连续激发，记录了5种球状蛋白[牛血清白蛋白（BSA），人血清白蛋白（HSA），核糖核酸酶A（RNase A），溶菌酶和胰蛋白酶]的自发荧光光谱。 5nm间隔。所获得的结果清楚地表明，由于在SDS处理后其二级和三级结构折叠的增加，BSA和HSA在其色氨酸部分周围发生了疏水塌陷。另一方面，胰蛋白酶在用SDS治疗后显示完全展开。经SDS处理后，溶菌酶和RNase A的自发荧光未显示任何差异，可能是由于它们的稳定性和荧光团组成所致。用特定的紫外线激发获得的上述结果清楚地表明，经SDS处理后，二级和三级结构的三级折叠和整体由其稳定性和稳定蛋白质的键支配。

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