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Nasri Nasrabadi, Nafiseh, Mohamadpour Dounighi, Naser, Najafi, Mojtaba, Ahmadinejad, Minoo, Bayatzadeh, Mohammad Ali, pouyanmehr, Giti, Vatanpour, Hossein, Vazife Shiran, Nader. (1402). Analysis and identification of Some Putative Novel Peptides purified from Iranian endemic Echis carinatus sochureki snake venom by MALDI-TOF Mass Spectrometry. سامانه مدیریت نشریات علمی, (), -. doi: 10.22092/ari.2023.361954.2701
Nafiseh Nasri Nasrabadi; Naser Mohamadpour Dounighi; Mojtaba Najafi; Minoo Ahmadinejad; Mohammad Ali Bayatzadeh; Giti pouyanmehr; Hossein Vatanpour; Nader Vazife Shiran. "Analysis and identification of Some Putative Novel Peptides purified from Iranian endemic Echis carinatus sochureki snake venom by MALDI-TOF Mass Spectrometry". سامانه مدیریت نشریات علمی, , , 1402, -. doi: 10.22092/ari.2023.361954.2701
Nasri Nasrabadi, Nafiseh, Mohamadpour Dounighi, Naser, Najafi, Mojtaba, Ahmadinejad, Minoo, Bayatzadeh, Mohammad Ali, pouyanmehr, Giti, Vatanpour, Hossein, Vazife Shiran, Nader. (1402). 'Analysis and identification of Some Putative Novel Peptides purified from Iranian endemic Echis carinatus sochureki snake venom by MALDI-TOF Mass Spectrometry', سامانه مدیریت نشریات علمی, (), pp. -. doi: 10.22092/ari.2023.361954.2701
Nasri Nasrabadi, Nafiseh, Mohamadpour Dounighi, Naser, Najafi, Mojtaba, Ahmadinejad, Minoo, Bayatzadeh, Mohammad Ali, pouyanmehr, Giti, Vatanpour, Hossein, Vazife Shiran, Nader. Analysis and identification of Some Putative Novel Peptides purified from Iranian endemic Echis carinatus sochureki snake venom by MALDI-TOF Mass Spectrometry. سامانه مدیریت نشریات علمی, 1402; (): -. doi: 10.22092/ari.2023.361954.2701

Analysis and identification of Some Putative Novel Peptides purified from Iranian endemic Echis carinatus sochureki snake venom by MALDI-TOF Mass Spectrometry

Archives of Razi Institute
مقالات آماده انتشار، پذیرفته شده، انتشار آنلاین از تاریخ 06 خرداد 1402
نوع مقاله: Original Articles
شناسه دیجیتال (DOI): 10.22092/ari.2023.361954.2701
نویسندگان
Nafiseh Nasri Nasrabadi1؛ Naser Mohamadpour Dounighi* 2؛ Mojtaba Najafi3؛ Minoo Ahmadinejad4؛ Mohammad Ali Bayatzadeh5؛ Giti pouyanmehr6؛ Hossein Vatanpour7؛ Nader Vazife Shiran8
1Pharmaceutical Sciences Research Centre, School of Pharmacy, Shahid Beheshti University of Medical Sciences, Tehran, Iran.First Athour.
2Razi institute
3Department of Molecular Genetic and Animal Breeding, Gorgan University of Agricultural Sciences and Natural Resources, Golestan, Iran.
4Blood Transfusion Research Center, Institute for Research and Education in Transfusion Medicine, Tehran, Iran
5Department of Venomous Animals and Anti-venom, Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization, Karaj, Iran
6Ph.D. student of toxicology, Tehran Islamic Azad University.
7Department of Toxicology, School of Pharmacy, Shahid Beheshti University of Medical Sciences, Tehran, Iran
8Shahid Beheshti University of Medical Sciences, Tehran, Iran
چکیده
Abstract

The Iranian Echis Carinatus (IEC) venom is an exclusive natural source of bio-substances for a wide range of purposes in the blood coagulation cascade. The present study for the first time was aimed to assess novel pro-coagulant, anti-coagulant and anti-platelet proteins, named EC1.5 (a), EC5.1 (b) and EC4 (a) from Iranian Echis Carinatus (IEC) venom. These peptides were purified by multi-step chromatography methods. Hematological properties were measured using activated clotting tests, platelet aggregation studies, and hemorrhage assessment. Subsequently, these proteins were identified through both their intact molecular mass and peptide mass fingerprint (PMF) using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF/MS). Multiple sequence alignments were performed by ClustalW, Bioedit software. Molegro Data Modeller (MDM) 3.0 software was used to predict the putative tertiary structure of proteins. EC1.5 (a), a single-band protein with a molecular mass of 66 and 55 kDa, was observed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis as a reduced and non-reduced state, respectively. Based on the Mascot results, we considered that EC1.5 (a) is a metalloproteinase of group ΙΙ which exhibited potent pro-coagulant activity. It is predicted that the EC1.5 (a) with hemorrhagic activity, potentially is a metalloproteinase/disintegrin region that constitutes the disintegrin-like domains. Our findings demonstrate that the disintegrin domain of EC1.5 (a) lacks platelet aggregation inhibitory activity. On the contrary, this factor shows the property of a platelet aggregation inducer. Also, the EC5.1 (b) was observed as a single-band protein with a molecular mass of 7.5 kDa. EC5.1 (b) showed both anti-coagulant and anti-platelet properties. Additionally, the structure of the EC5.1 (b) fraction is expected to be similar to that of phospholipase A2, while EC4 (a) structure is potentially very similar to that of Echistatin with 5 kDa molecular mass. We introduce the predicted structure of P-II snake venom metalloproteinase/ disintegrin domains, phospholipase A2 and Echistatin-like fractions. Further research is therefore needed to determine the complete structure of these novel fractions and elucidate their mechanism of action and future therapeutic applications of cardiovascular and homeostasis disorders.



Keywords: Hemorrhagic metalloproteinases, Platelet aggregation inducer, Disintegrin, Phospholipase A2, MALDI TOF/MS.
کلیدواژه‌ها
Hemorrhagic metalloproteinases؛ Platelet aggregation inducer؛ Disintegrin؛ Phospholipase A2؛ MALDI TOF/MS
عنوان مقاله [English]
تجزیه ، تحلیل وشناسایی پپتیدهای نوین خالص‌سازی شده از سم مار بومی ایران Echis carinatus sochureki توسط طیف‌سنجی جرمی MALDI-TOF
نویسندگان [English]
ناصر محمدپور دونیقی2؛
کلیدواژه‌ها [English]
متالوپروتئینازهای هموراژیک (متالوپروتئینازهای خونریزی دهنده), القا کننده تجمع پلاکتی, دیسینتگرین, فسفولیپاز A2, طیف سنجی جرمی
آمار
تعداد مشاهده مقاله: 2


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