蚕蛹蛋白源ace抑制多肽的结构鉴定及抑制机理研究化学工艺专业论文.docxVIP

进行分子对接。多肽Pl与ACE的Thrl66、Gin28 进行分子对接。多肽Pl与ACE的Thrl66、Gin28 1、Thr372、Asp377、Lys5 1 1、 His5 13、Tyr520等氨基酸残基形成氢键，多肽P2与ACE的Gln281、Ala356、 Glu403、Asp415、Lys511、Tyr520等氨基酸残基形成氢键。 (3)为获得具有更高ACE抑制活性的多肽，以多肽P1、多肽P2为基 础设计了一系列多肽，考察了C端氨基酸、N端氨基酸对ACE抑制活性的 影响，获得Gly—Asn—Pro—Trp-Trp(IC50为1 1．0 pg／mL)、Asn-Pro—Trp—Trp(IC50 为11．9岖JmL)、Trp—Phe(IC50为8．6肛g／mL)、Trp-Trp(IC50为4．2 ppJmL)、 Arg-Tyr-Leu-Met(IC50为8．5斗g／mL)、Arg—T)廿Leu—Arg(IC50为8．2肛g／mL)、 Tyr-Leu-Met(IC50为7．9 gg／mL)等具有较高ACE抑制活性的多肽。 关键词：蚕蛹蛋白血管紧张素转换酶抑制多肽抑制动力学分子对 接 lI 万方数据 STUDY STUDY 0N IDENTlFICATl0N AND MEC卧NIS_0F ANGIOTENSlN INHlBITORY PEPTlDE FROM SILI册R_ With the advantages of safe，non-toxic and SO on，angiotensin I-converting enzyme(ACE)inhibitory peptide from natural source has become one of the potential alternatives of antihypertensive drug and health care products．Basing on two ACE inhibitory peptides(P 1 and P2)，in this research，the amino acid sequences of P 1 and P2 were determined by MALDI TOF MS；the inhibition mechanisms were studied by inhibition kinetic and molecular docking，and a series of modified peptide with high ACE inhibitory activity were obtained．The main research results are as follows： (1)The amino acid sequences of P 1，P2 were determinted by MALDI TOF MS．The amino acid sequence of P 1 was Gly-Asn—Pro-Trp-Met(GNPWM)with a molecular weight of 603．76 u，and the amino acid sequence of P2 was Asn—Arg—Tyr—Leu-Arg(NRVLR)with a molecular weight of 720．88 u．Their IC50 were 1 2．6 1 pg／mL and 1 4．68斗g／mL，respectively．Their resistance to hi．gh processing temperatures and simulated gastrointestinal digestion environment were studied．P 1 had good thermal stability under the condition of 40。C，and could resist simulated digestion；P 1 had good thermal stability under the condition of 400C，but it could not resist simulated digestion． III 万方数据 (2)The (2)The inhibition mechanisms of P 1，P2 were studied．The inhibition of P 1， P2 on ACE were reversible inhibition，which were studied by inhibition kinetic； P 1 was a noncompetit