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首页> 外文期刊>Journal of Biomolecular Structure and Dynamics >The effect of putrescine on stability and structural properties of bovine serum albumin
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The effect of putrescine on stability and structural properties of bovine serum albumin

机译：Putrescine对牛血清白蛋白稳定性和结构性质的影响

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摘要

Serum albumins are the abounding proteins in plasma. Their most important characteristic is that they act as carriers for a type of compound, for example, different drugs. Bovine Serum Albumin (BSA) is a single-chain polypeptide with 583 amino acids. Polyamines such as putrescine can interact with negatively charged molecules. The effect of putrescine on the structure of bovine serum albumin has been surveyed utilizing the method of UV-Vis spectroscopy, Thermal stability, fluorescence spectroscopy, and molecular docking at temperature 298 K and 308 K at pH 7.4 using Tris-HCl as a buffer. The complex formation between putrescine and bovine serum albumin was discovered as alter in the absorbance at 280 nm. The amount of absorption increases with the addition of putrescine. The adding of putrescine alters the bovine serum albumin and decrements the hydrophobicity of the micro-environment of the Trp residues in the inner hydrophobic zone. The static kind of quenching process was chiefly contained within the quenching of intrinsic emission of the protein. The fluorescence quenching details (K-sv) for complex bovine serum albumin-putrescine revealed one binding site for putrescine. The negative amount of Gibbs free energy change (Delta G degrees) suggested the binding operation was spontaneous. Communicated by Ramaswamy H. Sarma
机译：血清白蛋白是血浆中丰富的蛋白质。它们最重要的特点是充当一种化合物的载体，例如不同的药物。牛血清白蛋白（BSA）是一种含有583个氨基酸的单链多肽。腐胺等多胺可以与带负电荷的分子相互作用。利用紫外可见光谱、热稳定性、荧光光谱和分子对接方法，在298K和308K温度下，以Tris-HCl为缓冲液，研究了腐胺对牛血清白蛋白结构的影响。在280nm处，腐胺与牛血清白蛋白形成的复合物的吸光度发生了变化。随着腐胺的加入，吸收量增加。腐胺的加入改变了牛血清白蛋白，降低了Trp残基内部疏水区微环境的疏水性。静态猝灭过程主要包含在蛋白质固有发射的猝灭中。复合牛血清白蛋白腐胺的荧光猝灭细节（K-sv）显示腐胺有一个结合位点。吉布斯自由能的负变化量（δG度）表明结合操作是自发的。由Ramaswamy H.Sarma传达

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