本研究采用表面等离子体共振技术,以血管紧张素转换酶(angiotensin I converting enzyme,ACE)为蛋白配体,分析马氏珠母贝肉蛋白酶解产物(protein hydrolysate of Pinctada martensii,PHPM)超滤组分与配体的结合情况,利用质谱鉴定结合肽...本研究采用表面等离子体共振技术,以血管紧张素转换酶(angiotensin I converting enzyme,ACE)为蛋白配体,分析马氏珠母贝肉蛋白酶解产物(protein hydrolysate of Pinctada martensii,PHPM)超滤组分与配体的结合情况,利用质谱鉴定结合肽段的氨基酸序列后,筛选潜在抑制ACE活性强的肽段进行合成,研究其体外ACE抑制活性、抑制类型及多肽与ACE蛋白的相互作用。结果显示,PHPM分子质量在3 000~5 000 Da的超滤组分与ACE蛋白具有较强的结合信号,在结合物质的肽序列中优选出4种具有潜在活性的ACE抑制肽进行合成,其中多肽SLPWPMKPMNLIE的半数抑制浓度最低,并且通过氢键与ACE蛋白C端结构域的疏水口袋结合。展开更多
The elucidation of key influence factors for electrostatic adsorption is very important to control protein nonspecific adsorption on modified surfaces. In this study, real time surface plasmon resonance technique is u...The elucidation of key influence factors for electrostatic adsorption is very important to control protein nonspecific adsorption on modified surfaces. In this study, real time surface plasmon resonance technique is used to characterize the electrostatic adsorption of two proteins (mouse IgG and protein A) on carboxymethyldextran modified surface. The results show that protein solution pH and ionic strength are key influence factors for efficient electrostatic adsorption. The influence of protein solution pH on the amount of electrostatic adsorption depends on the type of the charge and the charge density of both protein and modified matrix on the surface. The electrostatic adsorption process involves a competition between the positively charged protein and other positively charged species in the buffer solution. A decrease of ionic strength leads to an increasing electrostatic adsorption. The kinetic adsorption constants of protein A at different pH values were also calculated and compared.展开更多
文摘The elucidation of key influence factors for electrostatic adsorption is very important to control protein nonspecific adsorption on modified surfaces. In this study, real time surface plasmon resonance technique is used to characterize the electrostatic adsorption of two proteins (mouse IgG and protein A) on carboxymethyldextran modified surface. The results show that protein solution pH and ionic strength are key influence factors for efficient electrostatic adsorption. The influence of protein solution pH on the amount of electrostatic adsorption depends on the type of the charge and the charge density of both protein and modified matrix on the surface. The electrostatic adsorption process involves a competition between the positively charged protein and other positively charged species in the buffer solution. A decrease of ionic strength leads to an increasing electrostatic adsorption. The kinetic adsorption constants of protein A at different pH values were also calculated and compared.
