An amphipathic alpha-helical peptide from apolipoprotein A1 stabilizes protein polymer vesicles
نویسندگان
چکیده
منابع مشابه
Computer programs to identify and classify amphipathic alpha helical domains.
The amphipathic alpha helix is an often-encountered secondary structural motif in biologically active peptides and proteins. An amphipathic helix is defined as an alpha helix with opposing polar and nonpolar faces oriented along the long axis of the helix. In a recent review article we grouped amphipathic helixes into seven distinct classes (A, H, L, G, K, C, and M) based upon a detailed analys...
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To investigate the structure-function relationship of human apolipoprotein A-IV (apoA-IV), several deletion mutants of this protein were constructed by sequentially removing pairs of 22-residue repeats, potentially having an amphipathic alpha-helical conformation. The mutants, produced as recombinant poly-histidine-tagged apolipoproteins (t-apo) in Escherichia coli, assembled with phosphatidylc...
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The design of dimeric coiled-coils has ultimately led to novel applications, such as self-replicating peptide systems, whereas the structural features of the less common trimeric coiled-coil continue to be elucidated. Novel topologies have been discovered in designed proteins, as exemplified by the right-handed tetrameric coiled-coil and the inverted U four-helix bundle, and a single switch of ...
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The exchangeable apolipoproteins are important in determining the structure/function properties of lipoproteins. These proteins typically contain varying amounts of amphipathic helices. Five model peptides, 18A, Ac-18A-NH2, Ac-18R-NH2, 37pA, and 37aA, have been designed to investigate variations of the amphipathic alpha-helix structural motif on their lipid-binding properties. These include the...
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Apolipoprotein A-I is the most abundant protein in Cyprinus carpio plasma that plays an important role in lipid transport and protection of the skin by means of its antimicrobial activity. A 527 bp cDNA fragment encoding C terminus part of apoA-I from the skin mucosa of common carp was isolated using RT-PCR. After GenBank database searching, a partial sequence containing a coding sequence (CDS)...
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ژورنال
عنوان ژورنال: Journal of Controlled Release
سال: 2014
ISSN: 0168-3659
DOI: 10.1016/j.jconrel.2014.07.003