ارزیابی توان مهارکنندگی ناحیه پروپپتید به عنوان مهارگر کیموتریپسین گوارشی کرم غوزة پنبه،Helicoverpa armigera (Lepidoptera: Noctuidae)، بر اساس مطالعه ‏های محاسباتی

نوع مقاله : مقاله کامل، فارسی

نویسندگان

گروه گیاه ‏‏پزشکی، دانشکده کشاورزی، دانشگاه شهید چمران اهواز، اهواز، ایران

چکیده

کرم غوزه پنبه، Helicoverpa armigera Hübner، آفتی با دامنه میزبانی وسیع است که باعث خسارت اقتصادی شدید روی محصولات کشاورزی در ایران و جهان می ­‏شود. در سال­ های اخیر، حشره‏‏ کش‏‏ های شیمیایی به عنوان موثرترین روش کنترل این آفت استفاده شده ­اند، ‏که با توجه به اثرات مخرب آن‏‏ها، اغلب پژوهش ­ها در راستای دستیابی به روشی جایگزین برای کنترل شیمیایی هدایت می­‏ شوند. یکی از رویکرد‏های کارآمد برای کنترل آفات، هدف قرار دادن دستگاه گوارش و به ‏­ویژه مهار آنزیم ­‏های گوارشی می‏‏ باشد. در این مطالعه، ما از قطعة پروپپتید آنزیم کیموتریپسین H. armigera به عنوان یک مهارکننده اختصاصی استفاده نمودیم. مدل ساختاری کیموتریپسین حشره از طریق مدل‏‏ سازی همسانی و با استفاده از ساختار کریستالی کیموتریپسین گاوی، Bos taurus L. به عنوان ساختار الگو پیش­‏بینی شد. کیفیت مدل ساختاری حاصل توسط آنالیزهای مختلف از جملهVERIFY_3D ،ERRAT ، PROCHECK،WHAT-IF  و Z-scores مورد ارزیابی قرار گرفت، که نتایج نشان از کیفیت مطلوب مدل پیشنهادی داشت. علاوه بر این، مطالعات شبیه­‏سازی داکینگ مولکولی میان مدل ساختاری پیش‏­بینی شده آنزیم و پروپپتید مهار­کننده نشان داد که پروپپتید مهار‏کننده مطلوب‏‏ترین امتیاز داکینگ و انرژی پیوند کل را در هنگام برقرای میان­‏ کنش با جایگاه فعال کیموتریپسین کرم غوزه پنبه دارا می­‏ باشد. با این حال، پروپپتید مهار­کننده پتانسیل ضعیفی برای ایجاد میان ­‏کنش با کیموتریپسین خوکی، Sus scrofa L.، به عنوان نماینده­‏ای از پستانداران، از خود بروز داد. نتایج حاصل از این پژوهش، اهمیت مطالعه ‏های محاسباتی در طراحی و انتخاب پروپپتید­های مهاری مطلوب علیه آنزیم­‏ های هدف را نشان می‏دهد. چنین مهار­کننده ‏­هایی می‏­توانند به عنوان جایگزین آفت‏­ کش ­‏های شیمیایی برای کنترل H. armigera و یا سایر آفات در آینده پیشنهاد شوند.

کلیدواژه‌ها

عنوان مقاله [English]

Evaluation of the inhibitory potential of pro-peptide region as the inhibitor of the digestive chymotrypsin of cotton bollworm, Helicoverpa armigera (Lepidoptera: Noctuidae), based on in silico studies

نویسندگان [English]

  • S. A. Hemmati
  • N. Karam Kiani
Department of Plant Protection, Faculty of Agriculture, Shahid Chamran University of Ahvaz, Ahvaz, Iran
چکیده [English]

The cotton bollworm, Helicoverpa armigera (Hübner),is a wide host range pest that causes severe economic damages to agricultural crops in Iran and all around the world. During recent years, chemical insecticides have been used as the most effective strategy in control of this pest, but due to their hazardous effects, most of the researches are being conducted to offer an alternative approach for chemical control. In this regard, digestive systems, in particular inhibition of insect digestive enzymes, are considered as a target for pest control. Here, we used the original pro-region of H. armigera chymotrypsin as a potent and specific inhibitor of the pest enzyme. The structural model of the insect chymotrypsin was predicted based on homology modeling and the crystal structure of Bos taurus L. as template. The reliability of the model was assessed using VERIFY_3D, ERRAT, PROCHECK, WHAT-IF and Z-scores, and the results confirmed that the predicted structural model has an appropriate quality. Moreover, molecular docking simulations between the predicted structural model of enzyme and designed peptide showed that the inhibitor peptide has the most appropriate docking score and total binding energy for interactions with the insect chymotrypsin’s active site. However, it showed a weak potential for interaction with Sus scrofa L. chymotrypsin, as a representative of the mammalian enzyme. The results of this report indicate the importance of computational studies in design and selection of the favored inhibitor pro-peptides against the target enzymes. Such inhibitors can be further suggested as a replacement of chemical pesticides for controlling of H. armigera as well as the other pests in future.

کلیدواژه‌ها [English]

  • Helicoverpa armigera
  • Chymotrypsin
  • Homology modeling
  • Inhibitor peptide
  • Molecular docking simulation

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