CONTRIBUTION OF ELECTROSTATIC AND HYDROPHOBIC INTERACTIONS TO THE ADSORPTION OF PROTEINS BY ALUMINUM-CONTAINING ADJUVANTS
CONTRIBUTION OF ELECTROSTATIC AND HYDROPHOBIC INTERACTIONS TO THE ADSORPTION OF PROTEINS BY ALUMINUM-CONTAINING ADJUVANTS
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DOI：
10.1016/0264-410x(95)80009-3
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发表时间：
1995-01-01
期刊：
影响因子：
5.5
通讯作者：
HEM, SL
中科院分区：
文献类型：
--
作者：
ALSHAKHSHIR, RH;REGNIER, FE;HEM, SL
在pH 7.4和25℃条件下，研究了离子强度和乙二醇对市售氢氧化铝或磷酸铝佐剂吸附牛血清白蛋白(BSA)或溶菌酶的影响。氢氧化铝佐剂对牛血清白蛋白(BSA)的吸附和磷酸铝佐剂对溶菌酶的吸附与离子强度呈负相关，表明静电引力有助于吸附。添加乙二醇会降低磷酸铝佐剂对溶菌酶的吸附。然而，当乙二醇量高达40%时，氢氧化铝佐剂对牛血清白蛋白的吸附没有变化。这一行为表明疏水作用力有助于溶菌酶的吸附，而不是BSA的吸附。然而，当蛋白质和佐剂具有相同的表面电荷时，几乎没有观察到吸附。因此，如果存在静电排斥力，吸引力可能不足以产生含铝佐剂对抗原的吸附。
The effect of ionic strength and ethylene glycol on the adsorption of bovine serum albumin (BSA) or lysozyme by a commercial aluminium hydroxide or aluminium phosphate adjuvant was studied at pH 7.4 and 25 degrees C. The adsorption of BSA by aluminium hydroxide adjuvant and lysozyme by aluminium phosphate adjuvant was found to be inversely related to ionic strength, This indicates that electrostatic attractive forces contribute to adsorption. The adsorption of lysozyme by aluminium phosphate adjuvant was reduced by the addition of ethylene glycol. However, no change in the adsorption of BSA by aluminium hydroxide adjuvant was noted when up to 40% ethylene glycol was present. This behaviour indicates that hydrophobic forces contribute to the adsorption of lysozyme but not of BSA. However, virtually no adsorption was observed when the protein and the adjuvant had the same surface charge. Thus, attractive forces may not be sufficient to produce adsorption of an antigen by an aluminium-containing adjuvant if electrostatic repulsive forces are present.