Conformational Tuning of Amylin by Charged Styrene-Maleic-Acid Copolymers.

Szczegóły
Abstrakt

Tytuł:: Conformational Tuning of Amylin by Charged Styrene-Maleic-Acid Copolymers.
Autorzy:: Sahoo BR; Biophysics Program, The University of Michigan, Ann Arbor, MI 48109, USA; Department of Chemistry, Biomedical Engineering, and Macromolecular Science and Engineering, The University of Michigan, Ann Arbor, MI 48109, USA.
Souders CL 2nd; College of Veterinary Medicine, University of Florida, Gainesville, FL 32611, USA.
Watanabe-Nakayama T; Bio-AFM Frontier Research Center, Kanazawa University, Kanazawa 9201192, Japan.
Deng Z; Biophysics Program, The University of Michigan, Ann Arbor, MI 48109, USA.
Linton H; Department of Neurology, University of Michigan, Ann Arbor, MI 48109-2200, USA.
Suladze S; Department of Chemistry, Technische Universität München, Garching 85748, Germany.
Ivanova MI; Biophysics Program, The University of Michigan, Ann Arbor, MI 48109, USA; Department of Neurology, University of Michigan, Ann Arbor, MI 48109-2200, USA.
Reif B; Department of Chemistry, Technische Universität München, Garching 85748, Germany.
Ando T; Bio-AFM Frontier Research Center, Kanazawa University, Kanazawa 9201192, Japan.
Martyniuk CJ; Department of Chemistry, Biomedical Engineering, and Macromolecular Science and Engineering, The University of Michigan, Ann Arbor, MI 48109, USA.
Ramamoorthy A; Biophysics Program, The University of Michigan, Ann Arbor, MI 48109, USA; Department of Chemistry, Biomedical Engineering, and Macromolecular Science and Engineering, The University of Michigan, Ann Arbor, MI 48109, USA. Electronic address: .
Źródło:: Journal of molecular biology [J Mol Biol] 2022 Jan 30; Vol. 434 (2), pp. 167385. Date of Electronic Publication: 2021 Dec 06.
Typ publikacji:: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
Język:: English
Imprint Name(s):: Publication: Amsterdam : Elsevier
Original Publication: 1959- : London : Academic Press
MeSH Terms:: Molecular Conformation*
Islet Amyloid Polypeptide/*chemistry
Maleates/*chemistry
Styrene/*chemistry
Amyloid/chemistry ; Animals ; Computer Simulation ; Diabetes Mellitus, Type 2 ; Fluorescence ; Humans ; Hydrophobic and Hydrophilic Interactions ; Protein Aggregates ; Spectroscopy, Fourier Transform Infrared ; Styrenes/chemistry ; Zebrafish
References:: Diabetes. 2007 May;56(5):1324-32. (PMID: 17353506)
Proc Natl Acad Sci U S A. 2015 Jun 16;112(24):E3095-103. (PMID: 26038575)
Small. 2018 Nov;14(47):e1802825. (PMID: 30369028)
Chem Biol Drug Des. 2006 Jan;67(1):27-37. (PMID: 16492146)
J Biol Chem. 2012 Feb 17;287(8):5235-41. (PMID: 22187437)
Curr Opin Struct Biol. 2018 Feb;48:40-48. (PMID: 29080468)
Nat Commun. 2019 Jan 15;10(1):225. (PMID: 30644384)
FEBS Open Bio. 2012 Feb 28;2:20-5. (PMID: 23650576)
Cryo Letters. 2006 Sep-Oct;27(5):319-28. (PMID: 17256065)
Biochem J. 2016 Dec 1;473(23):4349-4360. (PMID: 27694389)
Chem Commun (Camb). 2020 Jun 18;56(48):6511-6514. (PMID: 32462144)
J Chem Theory Comput. 2011 Dec 13;7(12):4026-37. (PMID: 26598349)
J Biomol NMR. 2005 Dec;33(4):199-211. (PMID: 16341750)
Biochemistry. 2015 Jun 9;54(22):3555-64. (PMID: 25966003)
Biophys J. 2016 Jul 12;111(1):140-51. (PMID: 27410742)
J Mol Graph. 1996 Feb;14(1):33-8, 27-8. (PMID: 8744570)
Cell Death Differ. 2011 Mar;18(3):415-26. (PMID: 20814419)
Chem Commun (Camb). 2018 Nov 13;54(91):12883-12886. (PMID: 30379172)
Bioinformatics. 2013 Apr 1;29(7):845-54. (PMID: 23407358)
J Am Chem Soc. 2010 Jul 7;132(26):8973-83. (PMID: 20536124)
Biomacromolecules. 2017 Dec 11;18(12):4249-4260. (PMID: 29035554)
Angew Chem Int Ed Engl. 2020 Jul 27;59(31):12837-12841. (PMID: 31999880)
Mol Biosyst. 2014 May;10(5):1104-16. (PMID: 24595807)
Soft Matter. 2019 Oct 9;15(39):7934-7944. (PMID: 31539004)
Angew Chem Int Ed Engl. 2018 Jan 26;57(5):1342-1345. (PMID: 29232017)
Biomater Sci. 2017 Feb 28;5(3):485-493. (PMID: 28078343)
Chem Sci. 2017 Jul 1;8(7):5030-5040. (PMID: 28970890)
J Mol Biol. 2018 Oct 19;430(21):4230-4244. (PMID: 30170005)
Biophys J. 2013 Jan 8;104(1):173-84. (PMID: 23332070)
Am J Pathol. 2010 Feb;176(2):861-9. (PMID: 20042670)
J Phys Chem B. 2019 May 30;123(21):4562-4570. (PMID: 31050900)
Chem Sci. 2019 Feb 27;10(14):3976-3986. (PMID: 31015938)
ACS Appl Bio Mater. 2020 Oct 19;3(10):6598-6625. (PMID: 35019388)
Diabetes. 2013 Feb;62(2):327-35. (PMID: 23349537)
J Chem Inf Model. 2020 Dec 28;60(12):6462-6475. (PMID: 33174726)
FEBS Lett. 1990 Mar 26;262(2):279-81. (PMID: 2185950)
FEBS Lett. 2013 Apr 17;587(8):1106-18. (PMID: 23380070)
Biochemistry. 2008 Dec 2;47(48):12689-97. (PMID: 18989932)
Angew Chem Int Ed Engl. 2017 Sep 11;56(38):11466-11470. (PMID: 28714233)
Nanoscale. 2018 Nov 1;10(42):19995-20006. (PMID: 30350837)
Protein Expr Purif. 2015 Feb;106:49-56. (PMID: 25448593)
Proc Natl Acad Sci U S A. 2016 May 24;113(21):5835-40. (PMID: 27162352)
Biochemistry. 2005 Dec 13;44(49):16284-91. (PMID: 16331989)
Elife. 2016 May 23;5:. (PMID: 27213520)
J Chem Theory Comput. 2005 May;1(3):472-83. (PMID: 26641514)
Sci Rep. 2014 Mar 04;4:4267. (PMID: 24589570)
Diabetes. 2007 Jan;56(1):65-71. (PMID: 17192466)
Sci Rep. 2017 Mar 13;7:44041. (PMID: 28287098)
Diabetes Res Clin Pract. 1992 Jan;15(1):89-96. (PMID: 1541240)
J Am Chem Soc. 2009 May 27;131(20):7079-85. (PMID: 19405534)
Front Chem. 2019 Jul 30;7:480. (PMID: 31417892)
Grant Information:: R01 AG048934 United States AG NIA NIH HHS; R01 NS096785 United States NS NINDS NIH HHS
Contributed Indexing:: Keywords: IAPP; SMA copolymer; amylin; amyloid; type-II diabetes
Substance Nomenclature:: 0 (Amyloid)
0 (Islet Amyloid Polypeptide)
0 (Maleates)
0 (Protein Aggregates)
0 (Styrenes)
44LJ2U959V (Styrene)
91XW058U2C (maleic acid)
Entry Date(s):: Date Created: 20211209 Date Completed: 20220204 Latest Revision: 20240405
Update Code:: 20240405
PubMed Central ID:: PMC8752516
DOI:: 10.1016/j.jmb.2021.167385
PMID:: 34883118
: Czasopismo naukowe

Full Text Finder

Human amylin forms structurally heterogeneous amyloids that have been linked to type-2 diabetes. Thus, understanding the molecular interactions governing amylin aggregation can provide mechanistic insights in its pathogenic formation. Here, we demonstrate that fibril formation of amylin is altered by synthetic amphipathic copolymer derivatives of the styrene-maleic-acid (SMAQA and SMAEA). High-speed AFM is used to follow the real-time aggregation of amylin by observing the rapid formation of de novo globular oligomers and arrestment of fibrillation by the positively-charged SMAQA. We also observed an accelerated fibril formation in the presence of the negatively-charged SMAEA. These findings were further validated by fluorescence, SOFAST-HMQC, DOSY and STD NMR experiments. Conformational analysis by CD and FT-IR revealed that the SMA copolymers modulate the conformation of amylin aggregates. While the species formed with SMAQA are α-helical, the ones formed with SMAEA are rich in β-sheet structure. The interacting interfaces between SMAEA or SMAQA and amylin are mapped by NMR and microseconds all-atom MD simulation. SMAEA displayed π-π interaction with Phe23, electrostatic π-cation interaction with His18 and hydrophobic packing with Ala13 and Val17; whereas SMAQA showed a selective interaction with amylin's C terminus (residues 31-37) that belongs to one of the two β-sheet regions (residues 14-19 and 31-36) involved in amylin fibrillation. Toxicity analysis showed both SMA copolymers to be non-toxic in vitro and the amylin species formed with the copolymers showed minimal deformity to zebrafish embryos. Together, this study demonstrates that chemical tools, such as copolymers, can be used to modulate amylin aggregation, alter the conformation of species.
Competing Interests: Declaration of interests The polymers used in this study SMAEA and SMAQA are produced in the Ramamoorthy lab at Michigan. They are US patented.
(Copyright © 2021 Elsevier Ltd. All rights reserved.)

Informacja