کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1944266 1053199 2013 8 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
ATR-FTIR studies in pore forming and membrane induced fusion peptides
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
ATR-FTIR studies in pore forming and membrane induced fusion peptides
چکیده انگلیسی

Infrared (IR) spectroscopy has been shown to be very reliable for the characterization, identification and quantification of structural data. Particularly, the Attenuated Total Reflectance (ATR) technique which became one of the best choices to study the structure and organization of membrane proteins and membrane-bound peptides in biologically relevant membranes. An important advantage of IR spectroscopy is its ability to analyze material under a very wide range of conditions including solids, liquids and gases. This method allows elucidation of component secondary structure elements of a peptide or protein in a global manner, and by using site specific isotope labeling allows determination of specific regions. A few advantages in using ATR-FTIR spectroscopy include; a relatively simple technique, allow the determination of peptide orientation in the membrane, allow the determination of secondary structures of very small peptides, and importantly, the method is sensitive to isotopic labeling on the scale of single amino acids. Many studies were reported on the use of ATR-FTIR spectroscopy in order to study the structure and orientation of membrane bound hydrophobic peptides and proteins. The list includes native and de-novo designed peptides, as well as those derived from trans-membrane domains of various receptors (TMDs). The present review will focus on several examples that demonstrate the potential and the simplicity in using the ATR-FTIR approach to determine secondary structures of proteins and peptides when bound, inserted, and oligomerized within membranes. The list includes (i) a channel forming protein/peptide: the Ca2 + channel phospholamban, (ii) a cell penetrating peptide, (iii) changes in the structure of a transmembrane domain located within ordered and non-ordered domains, and (iv) isotope edited FTIR to directly assign structure to the membrane associated fusion peptide in context of a Key gp41 Structural Motif. Importantly, a unique advantage of infrared spectroscopy is that it allows a simultaneous study of the structure of lipids and proteins in intact biological membranes without an introduction of foreign perturbing probes. Because of the long IR wavelength, light scattering problems are virtually non-existent. This allows the investigation of highly aggregated materials or large membrane fragments. This article is part of a Special Issue entitled: FTIR in membrane proteins and peptide studies.

Figure optionsDownload high-quality image (68 K)Download as PowerPoint slideHighlights
► Basic background for ATR-FTIR studies
► Examples highlighting the simplicity and advantages in using ATR-FTIR studies.
► Using site specific mutations and 13C isotope labeled to study HIV-1 fusion peptide in the context of large portion of a protein

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Biomembranes - Volume 1828, Issue 10, October 2013, Pages 2306–2313
نویسندگان
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