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1392/9/30، جلد ۲، شماره ۱، صفحات -
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| عنوان فارسی |
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| چکیده فارسی مقاله |
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| کلیدواژههای فارسی مقاله |
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| عنوان انگلیسی |
Solid phase chemical Synthesis and Structure- Activity Study of Brevinin -2R and Analogues as Antimicrobial Peptides |
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| چکیده انگلیسی مقاله |
Abstract Brevinin-2R, as 25 amino acids peptide of the skin of Rana ridibunda frog, possesses potent antimicrobial and low hemolytic activity. It has an N-terminal hydrophilic region and a C-terminal loop that is delineated by an intra-disulfide bridge. In our study, Brevinin-2R and its diastereomer as well as its cyclic analogue were synthesized and characterized in order to investigate its structural features and biological implications. Both analogues showed lower antimicrobial activities compared to Brevinin-2R. In spite of Brevinin-2R peptide which shows low hemolytic activity, these analogues failed to show any hemolytic activity even at higher concentrations (up to 400 µg/ml). Based on proteolytic stability measurements, diastereomer and cyclic analogues displayed 90% and 60% residual antimicrobial activity, respectively, while antimicrobial activity of Brevinin-2R was 20%. Circular Dichroism (CD) Spectroscopy was conducted to investigate the structure-activity relationship. The CD analysis revealed that amphipathic α -helical conformation of the synthesized peptides is involved in antimicrobial effects. CD studies and HPLC based measurement of retention time using a reverse phase column indicated that the Brevinin-2R can form an amphipathic loop resulting in an enhanced hydrophobicity. This amphipathic characteristic can induce the α-helical structure in the membrane-mimetic environment. The hemolytic activity of Brevinin-2R and its analogues appeared to correlate with the retention time as well as the α-helicity. Accordingly, it seems that the combination of incorporating of D-amino acids into lytic peptides and their cyclization may result in developing new antimicrobial peptides with improved properties for treating infectious diseases. Keywords: Brevinin-2R; Antimicrobial peptide; Secondary structure; Hemolytic activity; Proteolytic stability; A549; MCF7 |
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| کلیدواژههای انگلیسی مقاله |
Keywords: Brevinin-2R; Antimicrobial peptide; Secondary structure; Hemolytic activity; Proteolytic stability; A549; MCF7 |
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| نویسندگان مقاله |
57045---57046---57047--- |
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| نشانی اینترنتی |
http://jmb.tums.ac.ir/index.php/jmb/article/viewArticle/118 |
| فایل مقاله |
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| کد مقاله (doi) |
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| زبان مقاله منتشر شده |
en |
| موضوعات مقاله منتشر شده |
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| نوع مقاله منتشر شده |
Articles |
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