CAJ | 학술논문

采用分子动力学模拟方法研究了疏水蛋白( HFBI)在亲水云母表面的吸附过程。通过6组平行的分子动力学模拟得到了2种不同的稳定吸附结构，即通过N端和通过亲水的α螺旋与表面吸附，得到了5种吸附残基。进一步用自适应偏置力方法计算了所有吸附残基与表面的结合自由能。结果表明，残基Lys是吸附过程的关键残基，即当HFBI通过含有Lys残基的α螺旋与云母表面作用时，其吸附构象最稳定。静电作用是吸附过程的主要驱动力。在该吸附结构中， HFBI的疏水面暴露在溶液中，有效降低了云母表面的润湿性。
채용분자동역학모의방법연구료소수단백( HFBI)재친수운모표면적흡부과정。통과6조평행적분자동역학모의득도료2충불동적은정흡부결구，즉통과N단화통과친수적α라선여표면흡부，득도료5충흡부잔기。진일보용자괄응편치력방법계산료소유흡부잔기여표면적결합자유능。결과표명，잔기Lys시흡부과정적관건잔기，즉당HFBI통과함유Lys잔기적α라선여운모표면작용시，기흡부구상최은정。정전작용시흡부과정적주요구동력。재해흡부결구중， HFBI적소수면폭로재용액중，유효강저료운모표면적윤습성。
Atomistic molecular dynamics( MD) simulations were conducted to elucidate the adsorption beha- vior of hydrophobin protein( HFBI) on the hydrophilic mica surface. Six independent simulations starting from three representative initial orientations of HFBI toward the surface were performed. The adsorbed patches are clustered into two classes, namely theα-helix and the N-terminal part. The main secon-dary structures of pro- tein were preserved in the entire course of adsorption due to four disulfide bonds. Furthermore, binding free energies of five different adsorbed residues were calculated employing the adaptive biasing force method. The results showed that Lys was the key residue for the adsorption. It can be deduced that the adsorption of HFBI via the α-helix part consisting of Gln36, Asn37, Lys50, and Thr51 is most energetically favored. Electrostatic interactions constitute the main driving forces responsible for the adsorption of HFBI on the mica surface. In the most stable adsorbed structure, the hydrophobic patch was exposed in the aqueous media, leading to the reduction of the wettability of mica.