مناقشة طالب الماجستير أحمد فرج الله من قسم الصيدلة التكنولوجية

ناقش بنجاح طالب الماجستير أحمد محمد فرج الله من قسم الصيدلة التكنولوجية اليوم الأثنين الموافق 7/11/2016م أطروحة الماجستير بعنوان:

تصميم بروتيني وتوصيف وظيفي لببتيد صناعي معدل ذو انشطة مضادة للبكتيريا موجبة الجرامية المعزولة سريريا والتي لها مقاومة لمعظم المضادات الحيوية

Proteomic design and functional characterization of a modified synthetic peptide with potent antimicrobial activity against clinical isolates of multidrug resistant Gram-positive Bacteria

وقد ضمت لجنة المناقشة  الدكتور عمار المعايطة رئيساً وعضوية كل من الدكتورة يارا التل والدكتورة نداء شريدة الدكتورة أريج عساف كممتحن خارجي. باسم صفحة أصدقاء كلية الصيدلة_ في جامعة العلوم والتكنولوجيا الأردنية نبارك للطالب أحمد فرج اللخ إتمامه درجة الماجستير في الصيدلة التكنولوجية بنجاح وتفوق متمنين له مزيدا من التقدم.

للإطلاع على ملخص الدراسة

The wide-scale misuse use of antibiotics for the treatment of human infections during the last few decades has led to a dramatic increase in the emergence of multidrug-resistant bacteria (MDRB) among various bacterial strains. Global research is currently focused on finding novel alternative agents with different mechanisms of action rather than the use of conventional antibiotics to counteract the threat of bacterial and biofilm infections. Host Defense peptides (HDPs) represent promising alternative agents for conventional antibiotics as these molecules exhibit a broad spectrum of activity against several microbial strains. Scorpion venoms contain a cocktail of bioactive peptides that display numerous biological activities. AamAP1, a novel HDP from the venom of the North African scorpion Androctonus amoeruxi had previously been found to display moderate broad spectrum antimicrobial activities against representative strains of Gram-positive, Gram-negative bacteria and yeast in the range of 20–150 μM. The peptide also displayed significant hemolytic activity against sheep erythrocytes at concentrations that were employed in the antimicrobial studies. Several structural determinants are responsible for the antimicrobial and cytolytic activity of host defense peptides. In our study, a novel synthetic peptide analogue named A3 from the naturally occurring scorpion venom host defense AamAP1 peptide, was designed by modifying the parent peptide in order to increase the net positive charge, percentage of helicity and optimize other physico-chemical parameters involved in host defense peptides activity. The A3 peptide has been found to display potent and selective in vitro antimicrobial activities against a wide range of clinical isolated multi-drug resistant Gram-positive bacteria. In the present study, the in vitro antimicrobial and anti-biofilm activities of the peptide alone and in combination with four different types of antibiotics were assessed against multi-drug resistant Gram-positive bacterial strains. Our results showed that most of the combination groups displayed a synergistic mode of action which resulted in decreasing the MIC value for A3 peptide to the nanomolar concentrations. These effective concentrations were associated with negligible toxicities on mammalian cells. The results of our study indicate that combinations of A3 peptide with conventional antibiotics may be pursued as a potential novel treatment strategy against MDRB and biofilm forming bacteria.