Rationally Designed Turn Promoting Mutation in the Amyloid-β Peptide Sequence Stabilizes Oligomers in Solution
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Mendeley | Further Information

{"title"=>"Rationally designed turn promoting mutation in the amyloid-β peptide sequence stabilizes oligomers in solution", "type"=>"journal", "authors"=>[{"first_name"=>"Jayakumar", "last_name"=>"Rajadas", "scopus_author_id"=>"23971332600"}, {"first_name"=>"Corey W.", "last_name"=>"Liu", "scopus_author_id"=>"26643579600"}, {"first_name"=>"Paul", "last_name"=>"Novick", "scopus_author_id"=>"47961338200"}, {"first_name"=>"Nicholas W.", "last_name"=>"Kelley", "scopus_author_id"=>"26024726100"}, {"first_name"=>"Mohammed", "last_name"=>"Inayathullah", "scopus_author_id"=>"24177821800"}, {"first_name"=>"Melburne C.", "last_name"=>"LeMieux", "scopus_author_id"=>"15842101800"}, {"first_name"=>"Vijay S.", "last_name"=>"Pande", "scopus_author_id"=>"7004966384"}], "year"=>2011, "source"=>"PLoS ONE", "identifiers"=>{"issn"=>"19326203", "scopus"=>"2-s2.0-79960683145", "pui"=>"362200145", "doi"=>"10.1371/journal.pone.0021776", "isbn"=>"10.1371/journal.pone.0021776", "sgr"=>"79960683145", "pmid"=>"21799748"}, "id"=>"b42f3d21-b2a4-3d25-955b-5c18458b974f", "abstract"=>"Enhanced production of a 42-residue beta amyloid peptide (Aβ(42)) in affected parts of the brain has been suggested to be the main causative factor for the development of Alzheimer's Disease (AD). The severity of the disease depends not only on the amount of the peptide but also its conformational transition leading to the formation of oligomeric amyloid-derived diffusible ligands (ADDLs) in the brain of AD patients. Despite being significant to the understanding of AD mechanism, no atomic-resolution structures are available for these species due to the evanescent nature of ADDLs that hinders most structural biophysical investigations. Based on our molecular modeling and computational studies, we have designed Met35Nle and G37p mutations in the Aβ(42) peptide (Aβ(42)Nle35p37) that appear to organize Aβ(42) into stable oligomers. 2D NMR on the Aβ(42)Nle35p37 peptide revealed the occurrence of two β-turns in the V24-N27 and V36-V39 stretches that could be the possible cause for the oligomer stability. We did not observe corresponding NOEs for the V24-N27 turn in the Aβ(21-43)Nle35p37 fragment suggesting the need for the longer length amyloid peptide to form the stable oligomer promoting conformation. Because of the presence of two turns in the mutant peptide which were absent in solid state NMR structures for the fibrils, we propose, fibril formation might be hindered. The biophysical information obtained in this work could aid in the development of structural models for toxic oligomer formation that could facilitate the development of therapeutic approaches to AD.", "link"=>"http://www.mendeley.com/research/rationally-designed-turn-promoting-mutation-amyloid%CE%B2-peptide-sequence-stabilizes-oligomers-solution", "reader_count"=>39, "reader_count_by_academic_status"=>{"Unspecified"=>2, "Professor > Associate Professor"=>2, "Researcher"=>13, "Student > Doctoral Student"=>3, "Student > Ph. D. Student"=>10, "Student > Master"=>5, "Student > Bachelor"=>1, "Lecturer > Senior Lecturer"=>1, "Professor"=>2}, "reader_count_by_user_role"=>{"Unspecified"=>2, "Professor > Associate Professor"=>2, "Researcher"=>13, "Student > Doctoral Student"=>3, "Student > Ph. D. Student"=>10, "Student > Master"=>5, "Student > Bachelor"=>1, "Lecturer > Senior Lecturer"=>1, "Professor"=>2}, "reader_count_by_subject_area"=>{"Unspecified"=>5, "Engineering"=>2, "Biochemistry, Genetics and Molecular Biology"=>3, "Mathematics"=>1, "Agricultural and Biological Sciences"=>11, "Medicine and Dentistry"=>1, "Neuroscience"=>1, "Physics and Astronomy"=>3, "Chemistry"=>10, "Computer Science"=>2}, "reader_count_by_subdiscipline"=>{"Engineering"=>{"Engineering"=>2}, "Medicine and Dentistry"=>{"Medicine and Dentistry"=>1}, "Neuroscience"=>{"Neuroscience"=>1}, "Chemistry"=>{"Chemistry"=>10}, "Physics and Astronomy"=>{"Physics and Astronomy"=>3}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>11}, "Computer Science"=>{"Computer Science"=>2}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>3}, "Mathematics"=>{"Mathematics"=>1}, "Unspecified"=>{"Unspecified"=>5}}, "reader_count_by_country"=>{"Czech Republic"=>1, "Denmark"=>1, "Malaysia"=>1, "France"=>1, "Germany"=>1, "Spain"=>1}, "group_count"=>3}

Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/752692"], "description"=>"<p>Aβ<sub>42</sub>WT takes beta-sheet rich fibrils (curve WT) while Aβ<sub>42</sub>Nle35p37 shows a large negative peak around 197 nm indicating disordered structure (curve Mut). Thioflavin T fluorescence of Aβ<sub>42</sub>WT and Aβ<sub>42</sub>Nle35p37 peptides are shown in the inset. Data was measured at 25°C.</p>", "links"=>[], "tags"=>["spectroscopy"], "article_id"=>423063, "categories"=>["Biological Sciences", "Biochemistry", "Chemistry", "Biophysics", "Neuroscience"], "users"=>["Jayakumar Rajadas", "Corey W. Liu", "Paul Novick", "Nicholas W. Kelley", "Mohammed Inayathullah", "Melburne C. LeMieux", "Vijay S. Pande"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0021776.g002", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_CD_spectroscopy_of_the_A_42_Nle35p37_and_A_946_42_WT_peptides_/423063", "title"=>"CD spectroscopy of the Aβ<sub>42</sub>Nle35p37 and Aβ<sub>42</sub>WT peptides.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-07-22 00:51:03"}
  • {"files"=>["https://ndownloader.figshare.com/files/752811"], "description"=>"<p>2D <sup>1</sup>H-<sup>1</sup>H spectra of Aβ<sub>42</sub>Nle35p37 (A, B, C) and Aβ<sub>21–43</sub>Nle35p37 (D, E, F). TOCSY of (NH-Hα) region of the Aβ<sub>42</sub>Nle35p37 (A) and Aβ<sub>21–43</sub>Nle35p37 (D). NOESY of (NH-Hα) region of Aβ<sub>42</sub>Nle35p37 (B) and Aβ<sub>21–43</sub>Nle35p37 (E). NOESY of (NH-NH) region of Aβ<sub>42</sub>Nle35p37 (C) and Aβ<sub>21–43</sub>Nle35p37 (F). Data was measured at 15°C in 10% DMSO-d<sub>6</sub>, PBS, pH 7.2.</p>", "links"=>[], "tags"=>["nmr", "proton", "spectra"], "article_id"=>423180, "categories"=>["Biological Sciences", "Biochemistry", "Chemistry", "Biophysics", "Neuroscience"], "users"=>["Jayakumar Rajadas", "Corey W. Liu", "Paul Novick", "Nicholas W. Kelley", "Mohammed Inayathullah", "Melburne C. LeMieux", "Vijay S. Pande"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0021776.g004", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Two_dimensional_NMR_proton_spectra_of_A_946_peptides_/423180", "title"=>"Two-dimensional NMR proton spectra of Aβ peptides.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-07-22 00:53:00"}
  • {"files"=>["https://ndownloader.figshare.com/files/752747"], "description"=>"<p>A) Representative 1.0×1.0-µm x-y, 10-nm total z-range AFM micrograph of Aβ<sub>42</sub>WT preparation. Observed are irregularly shaped and sized aggregate particles, some connected by fibrils. B) A surface plot of the boxed region of (A) clearly showing the aggregate with connected fibril. C) Representative 1.0×1.0-µm x-y, 10-nm total z-range AFM micrograph of Aβ<sub>42</sub>Nle35p37 preparation showing discrete globular aggregates of uniform size and density.</p>", "links"=>[], "tags"=>["images", "peptide"], "article_id"=>423117, "categories"=>["Biological Sciences", "Biochemistry", "Chemistry", "Biophysics", "Neuroscience"], "users"=>["Jayakumar Rajadas", "Corey W. Liu", "Paul Novick", "Nicholas W. Kelley", "Mohammed Inayathullah", "Melburne C. LeMieux", "Vijay S. Pande"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0021776.g003", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_AFM_images_of_A_946_peptide_preparations_/423117", "title"=>"AFM images of Aβ peptide preparations.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-07-22 00:51:57"}
  • {"files"=>["https://ndownloader.figshare.com/files/752950"], "description"=>"<p>1D proton spectra of the aromatic/amide regions of 1∶4 (A) and 4∶1 (B) mixtures of Aβ<sub>42</sub>Nle35p37∶Aβ<sub>42</sub>WT. (C) 2D <sup>1</sup>H-<sup>15</sup>N HSQC (Heteronuclear Single Quantum Coherence) experiment of the 4∶1 Aβ<sub>42</sub>Nle35p37∶Aβ<sub>42</sub>WT mixture (Aβ<sub>42</sub>WT uniformly <sup>15</sup>N-labeled), in 10% DMSO/PBS, pH 7.2, at 25°C. (D) 2D <sup>1</sup>H-<sup>1</sup>H TOCSY (NH-Hα) region of the 4∶1 Aβ<sub>42</sub>Nle35p37∶Aβ<sub>42</sub>WT mixture, in 10% DMSO/PBS, pH 7.2.</p>", "links"=>[], "tags"=>["two-dimensional", "nmr", "spectra", "peptide"], "article_id"=>423313, "categories"=>["Biological Sciences", "Biochemistry", "Chemistry", "Biophysics", "Neuroscience"], "users"=>["Jayakumar Rajadas", "Corey W. Liu", "Paul Novick", "Nicholas W. Kelley", "Mohammed Inayathullah", "Melburne C. LeMieux", "Vijay S. Pande"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0021776.g006", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_One_and_two_dimensional_NMR_spectra_of_A_946_peptide_mixtures_/423313", "title"=>"One- and two-dimensional NMR spectra of Aβ peptide mixtures.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-07-22 00:55:13"}
  • {"files"=>["https://ndownloader.figshare.com/files/753080"], "description"=>"<p>Chemical shift assignments of Aβ<sub>42</sub>Nle35p37.</p>", "links"=>[], "tags"=>["assignments"], "article_id"=>423447, "categories"=>["Biological Sciences", "Biochemistry", "Chemistry", "Biophysics", "Neuroscience"], "users"=>["Jayakumar Rajadas", "Corey W. Liu", "Paul Novick", "Nicholas W. Kelley", "Mohammed Inayathullah", "Melburne C. LeMieux", "Vijay S. Pande"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0021776.t001", "stats"=>{"downloads"=>1, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Chemical_shift_assignments_of_A_42_Nle35p37_/423447", "title"=>"Chemical shift assignments of Aβ<sub>42</sub>Nle35p37.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2011-07-22 00:57:27"}
  • {"files"=>["https://ndownloader.figshare.com/files/753046"], "description"=>"<p>Chemical shift assignments of Aß<sub>21–43</sub>Nle35p37.</p>", "links"=>[], "tags"=>["assignments"], "article_id"=>423416, "categories"=>["Biological Sciences", "Biochemistry", "Chemistry", "Biophysics", "Neuroscience"], "users"=>["Jayakumar Rajadas", "Corey W. Liu", "Paul Novick", "Nicholas W. Kelley", "Mohammed Inayathullah", "Melburne C. LeMieux", "Vijay S. Pande"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0021776.t002", "stats"=>{"downloads"=>1, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Chemical_shift_assignments_of_A_21_8211_43_Nle35p37_/423416", "title"=>"Chemical shift assignments of Aß<sub>21–43</sub>Nle35p37.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2011-07-22 00:56:56"}
  • {"files"=>["https://ndownloader.figshare.com/files/752637"], "description"=>"<p>Aromatic/amide regions of A) Aβ<sub>42</sub>WT and B) Aβ<sub>42</sub>Nle35p37 in 10% DMSO/PBS, pH 7.2, at 25°C.</p>", "links"=>[], "tags"=>["nmr", "proton", "spectra"], "article_id"=>423002, "categories"=>["Biological Sciences", "Biochemistry", "Chemistry", "Biophysics", "Neuroscience"], "users"=>["Jayakumar Rajadas", "Corey W. Liu", "Paul Novick", "Nicholas W. Kelley", "Mohammed Inayathullah", "Melburne C. LeMieux", "Vijay S. Pande"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0021776.g001", "stats"=>{"downloads"=>3, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_One_dimensional_NMR_proton_spectra_of_A_946_peptides_/423002", "title"=>"One-dimensional NMR proton spectra of Aβ peptides.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-07-22 00:50:02"}
  • {"files"=>["https://ndownloader.figshare.com/files/752888"], "description"=>"<p>5 structures were taken at 1 ns intervals from the computational structure refinements. Shown are the six residues around the turns (solid color rendering for the four residues around the turns, semi-transparent for the leading and trailing residues), backbone heavy-atoms shown for all residues, and side-chain heavy-atoms included for the four residues around the turns. (A) The V24-N27 turn is observed in most SS-NMR studies, and as show here has a conformation similar to previous unconstrained MD simulations. (B) The induced beta-turn from the d-Pro mutation, V36-V39, is clearly defined.</p>", "links"=>[], "tags"=>["refinement"], "article_id"=>423259, "categories"=>["Biological Sciences", "Biochemistry", "Chemistry", "Biophysics", "Neuroscience"], "users"=>["Jayakumar Rajadas", "Corey W. Liu", "Paul Novick", "Nicholas W. Kelley", "Mohammed Inayathullah", "Melburne C. LeMieux", "Vijay S. Pande"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0021776.g005", "stats"=>{"downloads"=>0, "page_views"=>2, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_NOE_refinement_ensembles_/423259", "title"=>"NOE refinement ensembles.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-07-22 00:54:19"}
  • {"files"=>["https://ndownloader.figshare.com/files/379102", "https://ndownloader.figshare.com/files/379119"], "description"=>"<div><p>Enhanced production of a 42-residue beta amyloid peptide (Aβ<sub>42</sub>) in affected parts of the brain has been suggested to be the main causative factor for the development of Alzheimer's Disease (AD). The severity of the disease depends not only on the amount of the peptide but also its conformational transition leading to the formation of oligomeric amyloid-derived diffusible ligands (ADDLs) in the brain of AD patients. Despite being significant to the understanding of AD mechanism, no atomic-resolution structures are available for these species due to the evanescent nature of ADDLs that hinders most structural biophysical investigations. Based on our molecular modeling and computational studies, we have designed Met35Nle and G37p mutations in the Aβ<sub>42</sub> peptide (Aβ<sub>42</sub>Nle35p37) that appear to organize Aβ<sub>42</sub> into stable oligomers. 2D NMR on the Aβ<sub>42</sub>Nle35p37 peptide revealed the occurrence of two β-turns in the V24-N27 and V36-V39 stretches that could be the possible cause for the oligomer stability. We did not observe corresponding NOEs for the V24-N27 turn in the Aβ<sub>21–43</sub>Nle35p37 fragment suggesting the need for the longer length amyloid peptide to form the stable oligomer promoting conformation. Because of the presence of two turns in the mutant peptide which were absent in solid state NMR structures for the fibrils, we propose, fibril formation might be hindered. The biophysical information obtained in this work could aid in the development of structural models for toxic oligomer formation that could facilitate the development of therapeutic approaches to AD.</p> </div>", "links"=>[], "tags"=>["rationally", "designed", "promoting", "mutation", "peptide", "stabilizes", "oligomers"], "article_id"=>134908, "categories"=>["Biological Sciences", "Biochemistry", "Chemistry", "Biophysics", "Neuroscience"], "users"=>["Jayakumar Rajadas", "Corey W. Liu", "Paul Novick", "Nicholas W. Kelley", "Mohammed Inayathullah", "Melburne C. LeMieux", "Vijay S. Pande"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0021776.s001", "https://dx.doi.org/10.1371/journal.pone.0021776.s002"], "stats"=>{"downloads"=>2, "page_views"=>12, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Rationally_Designed_Turn_Promoting_Mutation_in_the_Amyloid_Peptide_Sequence_Stabilizes_Oligomers_in_Solution/134908", "title"=>"Rationally Designed Turn Promoting Mutation in the Amyloid-β Peptide Sequence Stabilizes Oligomers in Solution", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2011-07-22 01:21:48"}

PMC Usage Stats | Further Information

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Relative Metric

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