Adsorption characteristics of P(3HB) depolymerase as evaluated by surface plasmon resonance and atomic force microscopy.

Adsorption characteristics of P(3HB) depolymerase as evaluated by surface plasmon resonance and atomic force microscopy.
复制标题

通过表面等离子体共振和原子力显微镜评估 P(3HB) 解聚酶的吸附特性。

DOI:
10.1021/bm800790q
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发表时间:
2008
期刊:
影响因子:
6.2
通讯作者:
M. Maeda
M. Maeda
中科院分区:
化学2区
文献类型:
--
作者:
N. Matsumoto;M. Fujita;T. Hiraishi;H. Abe;M. Maeda

文献摘要

被引文献

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从动力学和动力学的角度,研究了PickettiaT1聚[(R)-3-羟基丁酸酯](P(3HB))解聚酶对可生物降解脂肪族聚酯P(3HB)和聚L-乳酸(PLLA)表面的分子识别作用。为了确定P(3HB)解聚酶底物结合域(SBD)与不同化学结构的聚合物底物相互作用的动力学参数,采用表面等离子体共振(SPR)技术进行了研究。另一方面,利用P(3HB)解聚酶的SBD功能化的原子力显微镜(AFM)悬臂式针尖,测量了聚合物表面的解结力等力学参数。SPR和AFM测量表明,SBD对P(3HB)和PLLA具有很高的亲和力。根据动力学和动力学的结果,在唯象模型的基础上,揭示了SBD-聚合物相互作用的能势格局,并对相互作用的机理进行了讨论。
Molecular recognition of poly[(R)-3-hydroxybutyrate] (P(3HB)) depolymerase from Ralstonia pickettii T1 to the surfaces of biodegradable aliphatic polyesters such as P(3HB) and poly(L-lactic acid) (PLLA) was examined from the viewpoints of kinetics and dynamics. To determine the kinetic parameters on the interaction between the substrate-binding domain (SBD) of P(3HB) depolymerase and various polymer substrates with different chemical structures, surface plasmon resonance (SPR) measurements were performed. On the other hand, using an atomic force microscopic (AFM) cantilever tip functionalized with the SBD of P(3HB) depolymerase, the mechanical parameters such as unbinding force to the polymer surfaces were measured. Both the SPR and AFM measurements showed that the SBD has a high affinity to P(3HB) and PLLA. From the results of kinetics and dynamics, the energy potential landscape of SBD-polymer interaction was disclosed on the basis of a phenomenological model, and the mechanism of the interaction was discussed.