Structural design and characterization of a channel-forming peptide
A 16-residue polypeptide model with the sequence acetyl-YALSLAATLLKEAASL-OH was derived by rational de novo peptide design. The designed sequence consists of amino acid residues with high propensity to adopt an alpha helical conformation, and sequential order was arranged to produce an amphipathic s...
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th-mahidol.211722018-07-24T10:37:11Z Structural design and characterization of a channel-forming peptide Chartchai Krittanai Sakol Panyim Mahidol University Biochemistry, Genetics and Molecular Biology A 16-residue polypeptide model with the sequence acetyl-YALSLAATLLKEAASL-OH was derived by rational de novo peptide design. The designed sequence consists of amino acid residues with high propensity to adopt an alpha helical conformation, and sequential order was arranged to produce an amphipathic surface. The designed sequence was chemically synthesized using a solid-phase method and the polypeptide was purified by reverse-phase liquid chromatography. Molecular mass analysis by electro-spray ionization mass spectroscopy confirmed the correct designed sequence. Structural characterization by circular dichroism spectroscopy demonstrated that the peptide adopts the expected alpha helical conformation in 50% acetonitrile solution. Liposome binding assay using Small Unilamellar Vesicle (SUV) showed a marked release of entrapped glucose by interaction between the lipid membrane and the tested peptide. The channel-forming activity of the peptide was revealed by a planar lipid bilayer experiment. An analysis of the conducting current at various applied potentials suggested that the peptide forms a cationic ion channel with an intrinsic conductance of 188 pS. These results demonstrate that a simple rational de novo design can be successfully employed to create short peptides with desired structures and functions. 2018-07-24T03:37:11Z 2018-07-24T03:37:11Z 2004-07-31 Article Journal of Biochemistry and Molecular Biology. Vol.37, No.4 (2004), 460-465 12258687 2-s2.0-4444336017 https://repository.li.mahidol.ac.th/handle/123456789/21172 Mahidol University SCOPUS https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=4444336017&origin=inward |
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Biochemistry, Genetics and Molecular Biology Chartchai Krittanai Sakol Panyim Structural design and characterization of a channel-forming peptide |
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A 16-residue polypeptide model with the sequence acetyl-YALSLAATLLKEAASL-OH was derived by rational de novo peptide design. The designed sequence consists of amino acid residues with high propensity to adopt an alpha helical conformation, and sequential order was arranged to produce an amphipathic surface. The designed sequence was chemically synthesized using a solid-phase method and the polypeptide was purified by reverse-phase liquid chromatography. Molecular mass analysis by electro-spray ionization mass spectroscopy confirmed the correct designed sequence. Structural characterization by circular dichroism spectroscopy demonstrated that the peptide adopts the expected alpha helical conformation in 50% acetonitrile solution. Liposome binding assay using Small Unilamellar Vesicle (SUV) showed a marked release of entrapped glucose by interaction between the lipid membrane and the tested peptide. The channel-forming activity of the peptide was revealed by a planar lipid bilayer experiment. An analysis of the conducting current at various applied potentials suggested that the peptide forms a cationic ion channel with an intrinsic conductance of 188 pS. These results demonstrate that a simple rational de novo design can be successfully employed to create short peptides with desired structures and functions. |
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Mahidol University |
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Mahidol University Chartchai Krittanai Sakol Panyim |
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Article |
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Chartchai Krittanai Sakol Panyim |
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Chartchai Krittanai |
title |
Structural design and characterization of a channel-forming peptide |
title_short |
Structural design and characterization of a channel-forming peptide |
title_full |
Structural design and characterization of a channel-forming peptide |
title_fullStr |
Structural design and characterization of a channel-forming peptide |
title_full_unstemmed |
Structural design and characterization of a channel-forming peptide |
title_sort |
structural design and characterization of a channel-forming peptide |
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2018 |
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https://repository.li.mahidol.ac.th/handle/123456789/21172 |
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1763498085754863616 |