دورية أكاديمية

An Offset Patterned Cross-β Structure in Assemblies of C 3 -Symmetric Peptide Amphiphiles.

التفاصيل البيبلوغرافية
العنوان: An Offset Patterned Cross-β Structure in Assemblies of C 3 -Symmetric Peptide Amphiphiles.
المؤلفون: Zagorodko O; Polymer Therapeutics Lab, Centro de Investigación Príncipe Felipe, C/d'Eduardo Primo Yúfera, 3, 46012, Valencia, Spain.; Institute for Complex Molecular Systems (ICMS), Eindhoven University of Technology, P. O. Box 513, 5600 MB, Eindhoven, The Netherlands., Melnyk T; Polymer Therapeutics Lab, Centro de Investigación Príncipe Felipe, C/d'Eduardo Primo Yúfera, 3, 46012, Valencia, Spain.; Centro de Investigación, Biomédica en Red en Oncología (CIBERONC), Av. Monforte de Lemos, 3-5, 28029, Madrid, Spain., Nebot VJ; Polymer Therapeutics Lab, Centro de Investigación Príncipe Felipe, C/d'Eduardo Primo Yúfera, 3, 46012, Valencia, Spain.; Curapath, Av. Benjamín Franklin, 19, 46980, Paterna, Valencia, Spain., Dankers PYW; Institute for Complex Molecular Systems (ICMS), Eindhoven University of Technology, P. O. Box 513, 5600 MB, Eindhoven, The Netherlands., Vicent MJ; Polymer Therapeutics Lab, Centro de Investigación Príncipe Felipe, C/d'Eduardo Primo Yúfera, 3, 46012, Valencia, Spain.; Centro de Investigación, Biomédica en Red en Oncología (CIBERONC), Av. Monforte de Lemos, 3-5, 28029, Madrid, Spain.
المصدر: Chemistry (Weinheim an der Bergstrasse, Germany) [Chemistry] 2024 Feb 01; Vol. 30 (7), pp. e202303194. Date of Electronic Publication: 2023 Dec 11.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Wiley-VCH Country of Publication: Germany NLM ID: 9513783 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1521-3765 (Electronic) Linking ISSN: 09476539 NLM ISO Abbreviation: Chemistry Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Weinheim, Germany : Wiley-VCH
مواضيع طبية MeSH: Peptides*/chemistry , Amyloid*/chemistry, Protein Structure, Secondary ; Protein Conformation, beta-Strand ; Phenylalanine
مستخلص: Developing peptide-based materials with controlled morphology is a critical theme of soft matter research. Herein, we report the formation of a novel, patterned cross-β structure formed by self-assembled C 3 -symmetric peptide amphiphiles based on diphenylalanine and benzene-1,3,5-tricarboxamide (BTA). The cross-β motif is an abundant structural element in amyloid fibrils and aggregates of fibril-forming peptides, including diphenylalanine. The incorporation of topological constraints on one edge of the diphenylalanine fragment limits the number of β-strands in β-sheets and leads to the creation of an unconventional offset-patterned cross-β structure consisting of short 3×2 parallel β-sheets stabilized by phenylalanine zippers. In the reported assembly, two patterned cross-β structures bind parallel arrays of BTA stacks in a superstructure within a single-molecule-thick nanoribbon. In addition to a threefold network of hydrogen bonds in the BTA stack, each molecule becomes simultaneously bound by hydrogen bonds from three β-sheets and four phenylalanine zippers. The diffuse layer of alkyl chains with terminal polar groups prevents the nanoribbons from merging and stabilizes cross-β-structure in water. Our results provide a simple approach to the incorporation of novel patterned cross-β motifs into supramolecular superstructures and shed light on the general mechanism of β-sheet formation in C 3 -symmetric peptide amphiphiles.
(© 2023 Wiley-VCH GmbH.)
References: R. Gallardo, N. A. Ranson, S. E. Radford, Curr. Opin. Struct. Biol. 2020, 60, 7-16.
M. R. Sawaya, S. Sambashivan, R. Nelson, M. I. Ivanova, S. A. Sievers, M. I. Apostol, M. J. Thompson, M. Balbirnie, J. J. W. Wiltzius, H. T. McFarlane, A. Madsen, C. Riekel, D. Eisenberg, Nature 2007, 447, 453-457.
T. R. Jahn, O. S. Makin, K. L. Morris, K. E. Marshall, P. Tian, P. Sikorski, L. C. Serpell, J. Mol. Biol. 2010, 395, 717-727.
S. Sieste, T. Mack, E. Lump, M. Hayn, D. Schütz, A. Röcker, C. Meier, K. Kaygisiz, F. Kirchhoff, T. P. J. Knowles, F. S. Ruggeri, C. V. Synatschke, J. Münch, T. Weil, Adv. Funct. Mater. 2021, 31, 2009382.
C. J. Bowerman, B. L. Nilsson, Biopolymers 2012, 98, 169-184.
A. Dasgupta, D. Das, Langmuir 2019, 35, 10704-10724.
R. Freeman, M. Han, Z. Álvarez, J. A. Lewis, J. R. Wester, N. Stephanopoulos, M. T. McClendon, C. Lynsky, J. M. Godbe, H. Sangji, E. Luijten, S. I. Stupp, Science 2018, 362, 808-813.
R. Wakabayashi, A. Suehiro, M. Goto, N. Kamiya, Chem. Commun. 2019, 55, 640-643.
M. P. Hendricks, K. Sato, L. C. Palmer, S. I. Stupp, Acc. Chem. Res. 2017, 50, 2440-2448.
A. Dehsorkhi, V. Castelletto, I. W. Hamley, J. Pept. Sci. 2014, 20, 453-467.
Y. Li, F. Wang, H. Cui, Bioeng. Transl. Med. 2016, 1, 306-322.
J. G. Ray, A. J. Johnson, D. A. Savin, J. Polym. Sci. Part B 2013, 51, 508-523.
S.-Y. Qin, H.-F. Jiang, M.-Y. Peng, Q. Lei, R.-X. Zhuoa, X.-Z. Zhang, Polym. Chem. 2015, 6, 519-524.
S. Cantekin, F. A. De Greef, A. R. A. Palmans, Chem. Soc. Rev. 2012, 6125-6137.
R. P. M. Lafleur, S. Herziger, S. M. C. Schoenmakers, A. D. A. Keizer, J. Jahzerah, B. N. S. Thota, L. Su, P. H. H. Bomans, N. A. J. M. Sommerdijk, A. R. A. Palmans, R. Haag, H. Friedrich, C. Bottcher, E. W. Meijer, J. Am. Chem. Soc. 2020, 142, 17644-17652.
S. M. C. Schoenmakers, A. J. H. Spiering, S. Herziger, C. Böttcher, R. Haag, A. R. A. Palmans, E. W. Meijer, ACS Macro Lett. 2022, 11, 711-715.
N. Stergiou, M. Urschbach, H. Yurugi, D. Spitzer, D. Schollmeyer, E. Schmitt, P. Besenius, ChemBioChem 2018, 19, 912-916.
P. Besenius, J. L. M. Heynens, R. Straathof, M. M. L. Nieuwenhuizen, P. H. H. Bomans, E. Terreno, S. Aime, G. J. Strijkers, K. Nicolay, E. W. Meijer, Contrast Media Mol. Imaging 2012, 7, 356-361.
O. Zagorodko, V. J. Nebot, M. J. Vicent, Polym. Chem. 2020, 11, 1220-1229.
L. Li, L. Wu, M. Urschbach, D. Straßburger, X. Liu, P. Besenius, G. Chen, ACS Polym. Au 2022, 2, 478-485.
O. Zagorodko, T. Melnyk, O. Rogier, V. J. Nebot, M. J. Vicent, Polym. Chem. 2021, 12, 3478-3487.
H. Frisch, J. P. Unsleber, D. Lüdeker, M. Peterlechner, G. Brunklaus, M. Waller, P. Besenius, Angew. Chem. Int. Ed. 2013, 52, 10097-10101.
D. L. Sackett, J. Wolff, Anal. Biochem. 1987, 167, 228-234.
C. Gao, S. Kewalramani, D. M. Valencia, H. Li, J. M. McCourt, M. O. De La Cruz, M. J. Bedzyk, Proc. Natl. Acad. Sci. USA 2019, 116, 22030-22036.
K. M. Vonk, E. W. Meijer, G. Vantomme, Chem. Sci. 2021, 12, 13572-13579.
H. Hiramatsu, T. Kitagawa, Biochim. Biophys. Acta 2005, 1753, 100-107.
L. E. Uche, G. S. Gooris, J. Bouwstra, C. M. Beddoes, Langmuir 2019, 35, 15376-15388.
G. Zandomeneghi, M. R. H. Krebs, M. G. McCammon, M. Fändrich, Protein Sci. 2009, 13, 3314-3321.
F. Vosough, A. Barth, ACS Chem. Neurosci. 2021, 12, 473-488.
W. Haitao, Y. Yang, X. Huang, Y. Zhu, H. Wang, G. Huang, J. Wu, J. Mater. Chem. A 2020, 8, 9013-9020.
A. Barth, Biochim. Biophys. Acta Bioenerg. 2007, 1767, 1073-1101.
C. M. A. Leenders, M. B. Baker, I. A. B. Pijpers, R. P. M. Lafleur, L. Albertazzi, A. R. A. Palmans, E. W. Meijer, Soft Matter 2016, 12, 2887-2893.
S. D. Moran, M. T. Zanni, J. Phys. Chem. Lett. 2014, 5, 1984-1993.
M. Reches, E. Gazit, Curr. Nanosci. 2006, 2, 105-111.
R. N. A. H. Lewis, R. N. McElhaney, Biochim. Biophys. Acta Biomembr. 2013, 1828, 2347-2358.
H. H. Mantsch, C. Madec, Biochemistry 1985, 24, 2440-2446.
E. Peggion, M. Palumbo, G. M. Bonora, C. Toniolo, Bioorg. Chem. 1974, 3, 125-132.
J. Bürck, P. Wadhwani, S. Fanghänel, A. S. Ulrich, Acc. Chem. Res. 2016, 49, 184-192.
M. J. B. Tunis-Schneider, M. F. Maestre, J. Mol. Biol. 1970, 52, 521-541.
R. W. Woody, Tetrahedron: Asymmetry 1993, 4, 529-544.
S. I. S. Hendrikse, L. Su, T. P. Hogervorst, R. P. M. Lafleur, X. Lou, G. A. Van Der Marel, J. D. C. Codee, E. W. Meijer, J. Am. Chem. Soc. 2019, 141, 13877-13886.
M. Sunde, L. C. Serpell, M. Bartlam, P. E. Fraser, M. B. Pepys, C. C. F. Blake, J. Mol. Biol. 1997, 273, 729-739.
X. Li, F. Wei, X. Le, L. Wang, D. Wang, C. Chen, S. Xu, X. Liao, Y. Zhao, J. Mol. Liq. 2022, 355, 118940.
A. M. Garcia, M. Melchionna, O. Bellotto, S. Kralj, S. Semeraro, E. Parisi, D. Iglesias, P. D. Andrea, R. De Zorzi, A. V. Vargiu, S. Marchesan, ACS Nano 2021, 15, 3015-3025.
I. W. Hamley, A. Dehsorkhi, V. Castelletto, Langmuir 2013, 29, 5050-5059.
K. Manalastas-Cantos, P. V. Konarev, N. R. Hajizadeh, A. G. Kikhney, M. V. Petoukhov, D. S. Molodenskiy, A. Panjkovich, H. D. T. Mertens, A. Gruzinov, C. Borges, C. M. Jeffries, D. I. Svergun, D. Franke, J. Appl. Crystallogr. 2021, 54, 343-355.
معلومات مُعتمدة: PID2019-108806RB-I00 Ministerio de Economía y Competitividad; ERC-CoG-2014-648831 MyNano HORIZON EUROPE European Research Council; Gravity Program 024.005.020 Ministerie van Onderwijs, Cultuur en Wetenschap; EyeSciTe Chemelot InSciTe; PRDVA17201MELN Fundación Científica Asociación Española Contra el Cáncer; PO FEDER of Comunitat Valenciana, 2014 - 2020 Generalitat Valenciana
فهرسة مساهمة: Keywords: benzene-1,3,5-tricarboxamide; cross-beta; peptide amphiphiles; self-assembly; supramolecular polymers
المشرفين على المادة: 0 (Peptides)
0 (Amyloid)
47E5O17Y3R (Phenylalanine)
تواريخ الأحداث: Date Created: 20231115 Date Completed: 20240205 Latest Revision: 20240205
رمز التحديث: 20240205
DOI: 10.1002/chem.202303194
PMID: 37967312
قاعدة البيانات: MEDLINE
الوصف
تدمد:1521-3765
DOI:10.1002/chem.202303194