期刊
JOURNAL OF PHYSICAL CHEMISTRY B
卷 123, 期 41, 页码 8617-8627出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpcb.9b03276
关键词
-
资金
- Universidad Tecnologica Nacional [PID 5173]
- Universidad Nacional de San Luis (Argentina) [22116]
- CONICET (Argentina) [PIP 11220130100448CO]
- National Agency of Scientific and Technological Promotion (Argentina) [PICT-2016-4365, PICT 2017-0937]
Complexation between the beta-lactoglobulin and a weak acid polyelectrolyte (PE) has been studied using Monte Carlo simulations. Different coarse-grained models were used to represent the system, and two different acidic constants were used on the PE model. The protein-PE interaction is quantified considering the average PE monomers adsorbed on the protein as a function of pH. A maximum in the interaction between macromolecules was found, which is explained as a function of the titration behavior of the beta-lactoglobuline and weak PE. We also found that there was a direct relation between the pH range of monomers adsorbed and the change on dissociation profile of the protein and weak PE compared to isolated conditions. The complexation of protein PE increased both the dissociation degree of the PE chain and the protein net charge. This benefits the monomer adsorption on the protein surface.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据