亲木质素多肽的设计及其与苯丙烷二聚体的分子对接  

Design of Lignin-Binding Polypeptides for Molecular Docking with Dimeric Phenylpropanoids

作　　者：耿青杰 孙见良 杨文萍 刘浩[1] 李兵云[1] 付时雨[1] GENG Qing-jie;SUN Jian-liang;YANG Wen-ping;LIU Hao;LI Bing-yun;FU Shi-yu(State Key Laboratory of Pulp and Paper Engineering,South China University of Technology,Guangzhou 510640,China;School of Mathematics,South China University of Technology,Guangzhou 510640,China)

机构地区：[1]华南理工大学制浆造纸工程国家重点实验室,广东广州510640 [2]华南理工大学数学学院,广东广州510640

出　　处：《造纸科学与技术》2018年第5期74-78,共5页Paper Science & Technology

基　　金：国家自然科学基金项目(31570569);广东省基金博士启动纵向协同创新项目(2017A030310341);广州市科技计划项目(201607020025);制浆造纸工程国家重点实验室项目(2017QN01)

摘　　要：用多肽"阻隔"木质素是一种减少纤维素酶无效结合的新技术。本研究设计了10个多肽序列并构建了三维模型,其中序列FPLGPNHTNPSF与松柏醇和芥子醇的二聚体具有较高的亲和力,该序列中的天冬酰胺与木质素芳核的酚羟基和甲氧基通过氢键连接,其亮氨酸、组氨酸和苏氨酸则与木质素的苯环和脂肪链形成疏水作用。该序列与苯丙烷二聚体的结合能低于Trichoderma reesei纤维素酶的纤维素结合域(CBM),可用于"阻隔"木质素对纤维素酶的无效结合。Polypeptides have been proposed as a new type of blocking agents for eliminating the non-productive binding of cellulases onto lignin. In this work, 10 polypeptide sequences were designed and modelized, in which FPLGPNHTNPSF showed optimal affinity to dimers of coniferyl alcohol and sinapyl alcohol. Two asparagine residues in this sequence formed strong hydrogen bonds with the phenolic and methoxyl groups in the aromatic cores. The leucine, histidine and threonine interacted with the ring and aliphatic chain of lignin model compounds through hydrophobie interactions. The selected sequence had a lower binding energy with these dimerie phenylpropanoids than CBM from Trichoderma reese cellulase. It can thus be used to block the lignin-induced non-productive binding of cellulases.

关 键 词：多肽 木质素 亲和性 苯丙烷二聚体 分子对接 

分 类 号：R978.16[医药卫生—药品]