Interaction of Linear Polyelectrolytes with Proteins: Role of Specific Charge-Charge Interaction and Ionic Strength.
Interaction of Linear Polyelectrolytes with Proteins: Role of Specific Charge-Charge Interaction and Ionic Strength.
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DOI：
10.3390/biom11091377
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发表时间：
2021-09-17
期刊：
影响因子：
5.5
通讯作者：
Weinhart M
中科院分区：
文献类型：
--
作者：
Bukala J;Yavvari P;Walkowiak JJ;Ballauff M;Weinhart M
我们提出了一个合成的，线性聚电解质与牛血清白蛋白（BSA）的相互作用的热力学研究。所有聚电解质均基于聚（烯丙基缩水甘油醚），其已通过与阴离子（-SO 3 Na）、阳离子（-NH3 Cl或-NHMe 2Cl）或两性离子基团（-NMe 2（CH 2）3SO 3）的聚合物类似反应改性。虽然阴离子聚合物显示出非常弱的相互作用，但两性离子聚合物在所施加的pH = 7.4、离子强度（I = 23-80 mM）和温度条件（T = 20-37 ℃）下不表现出与BSA的相互作用（pI = 4.7）。一个强大的结合，然而，观察到的聚阳离子轴承伯氨基或叔二甲基氨基，这可以详细分析等温滴定量热法（ITC）。分析是使用一个表达式来完成的，该表达式描述了结合自由能ΔGb，作为两个决定性变量的函数，温度T和盐浓度cs。基础模型将ΔGb分为与CO2释放相关的项和与水释放相关的项。虽然两种体系释放的抗衡离子的数量相似，但与N，N-二甲基叔胺呈递聚合物相比，伯胺的结合水的释放更重要。这一发现进一步追溯到与体积较大的质子化叔胺基团相比，复合物中聚合物的质子化伯氨基基团与BSA的带相反电荷的部分的更紧密接触。因此，我们提出了一个调查，量化两个驱动力的静电结合，即counterweight的释放和水合作用的变化，这有助于更深入的理解，直接影响未来的进展，在生物医学领域。
We present a thermodynamic study of the interaction of synthetic, linear polyelectrolytes with bovine serum albumin (BSA). All polyelectrolytes are based on poly(allyl glycidyl ether) which has been modified by polymer-analogous reaction with anionic (-SO3Na), cationic (-NH3Cl or -NHMe2Cl) or zwitterionic groups (-NMe2(CH2)3SO3). While the anionic polymer shows a very weak interaction, the zwitterionic polymer exhibits no interaction with BSA (pI = 4.7) under the applied pH = 7.4, ionic strength (I = 23–80 mM) and temperature conditions (T = 20–37 °C). A strong binding, however, was observed for the polycations bearing primary amino or tertiary dimethyl amino groups, which could be analysed in detail by isothermal titration calorimetry (ITC). The analysis was done using an expression which describes the free energy of binding, ΔGb, as the function of the two decisive variables, temperature, T, and salt concentration, cs. The underlying model splits ΔGb into a term related to counterion release and a term related to water release. While the number of released counter ions is similar for both systems, the release of bound water is more important for the primary amine compared to the tertiary N,N-dimethyl amine presenting polymer. This finding is further traced back to a closer contact of the polymers’ protonated primary amino groups in the complex with oppositely charged moieties of BSA as compared to the bulkier protonated tertiary amine groups. We thus present an investigation that quantifies both driving forces for electrostatic binding, namely counterion release and change of hydration, which contribute to a deeper understanding with direct impact on future advancements in the biomedical field.
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影响因子：
4.4
作者：
MANNING, GS
通讯作者：
MANNING, GS
影响因子：
5.5
作者：
Gervais, Matthieu;Brocas, Anne-Laure;Carlotti, Stephane
通讯作者：
Carlotti, Stephane
影响因子：
3.9
作者：
Bergqvist, S;Williams, MA;Ladbury, JE
通讯作者：
Ladbury, JE
影响因子：
3.8
作者：
Liu, YF;Sturtevant, JM
通讯作者：
Sturtevant, JM
影响因子：
4.4
作者：
MANNING, GS
通讯作者：
MANNING, GS