کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
10870205 1073992 2014 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Structural features of peptoid-peptide hybrids in lipid-water interfaces
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
Structural features of peptoid-peptide hybrids in lipid-water interfaces
چکیده انگلیسی
The inclusion of peptoid monomers into antimicrobial peptides (AMPs) increases their proteolytic resistance, but introduces conformational flexibility (reduced hydrogen bonding ability and cis/trans isomerism). We here use NMR spectroscopy to answer how the insertion of a peptoid monomer influences the structure of a regular α-helical AMP upon interaction with a dodecyl phosphocholine (DPC) micelle. Insertion of [(2-methylpropyl)amino]acetic acid in maculatin-G15 shows that the structural change and conformational flexibility depends on the site of insertion. This is governed by the micelle interaction of the amphipathic helices flanking the peptoid monomer and the side chain properties of the peptoid and its preceding residue.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 588, Issue 17, 25 August 2014, Pages 3291-3297
نویسندگان
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