Integration of functional peptides into nucleic acid-based nanostructures
Source abstract
Abstract
In many applications such as diagnostics and therapy development, small peptide fragments consisting of only a few amino acids are often attractive alternatives to bulky proteins. This is due to factors such as the ease of scalable chemical synthesis and numerous methods for their discovery. One drawback of using peptides is that their activity can often be negatively impacted by the lack of a rigid, 3D stabilizing structure provided by the rest of the protein. In many cases, this can be alleviated by different methods of rational templating onto nanomaterials, which provides additional possibilities to use concepts of multivalence or rational nano-engineering to enhance or even create new types of function or structure. In recent years, nanostructures made from the self-assembly of DNA strands have been used as scaffolds to create functional arrangements of peptides, often leading to greatly enhanced biological activity or new material properties. This review will give an overview of nano-templating approaches based on the combination of DNA nanotechnology and peptides. This will include both bioengineering strategies to control interactions with cells or other biological systems, as well as examples where the combination of DNA and peptides has been leveraged for the rational design of new functional materials.
Source: openalex_inverted_index · Quality: candidate unverified · Source record ↗
Research context
OpenAlex topics: Advanced biosensing and bioanalysis techniques · RNA Interference and Gene Delivery · Supramolecular Self-Assembly in Materials
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Fraunhofer Institute for Cell Therapy and Immunology, 04103 Leipzig, Germany
Peter Debye Institute for Soft Matter Physics, Leipzig University, 04103 Leipzig, Germany
Unconventional Computing Lab, UWE, Bristol, BS16 1QY, UK
Institute of Clinical Immunology, University of Leipzig Medical Faculty, 04103 Leipzig, Germany
Funding
Fraunhofer-Gesellschaft · Bundesministerium für Bildung und Forschung
References (100+)
Show source-provided references
1. Merrifield · J. Am. Chem. Soc. · 1963 · 85 · 214910.1021/ja00897a025 ↗
2. Mitchell · Biopolymers · 2008 · 90 · 17510.1002/bip.20925 ↗
3. Sato · Curr. Opin. Biotechnol. · 2006 · 17 · 63810.1016/j.copbio.2006.10.002 ↗
4. Hamley · Chem. Rev. · 2017 · 117 · 1401510.1021/acs.chemrev.7b00522 ↗
5. Bellis · Biomaterials · 2011 · 32 · 420510.1016/j.biomaterials.2011.02.029 ↗
6. Miura · ACS Nano · 2013 · 7 · 858310.1021/nn402662d ↗
7. Hersel · Biomaterials · 2003 · 24 · 438510.1016/S0142-9612(03)00343-0 ↗
8. Houghten · Proc. Natl. Acad. Sci. U. S. A. · 1985 · 82 · 513110.1073/pnas.82.15.5131 ↗
9. Alhoot · Int. J. Med. Sci. · 2013 · 10 · 71910.7150/ijms.5037 ↗
10. Smith · Science · 1985 · 228 · 131510.1126/science.4001944 ↗
11. Memczak · PLoS One · 2016 · 11 · e015907410.1371/journal.pone.0159074 ↗
12. Pelay-Gimeno · Angew. Chem., Int. Ed. · 2015 · 54 · 889610.1002/anie.201412070 ↗
13. Grillaud · J. Pept. Sci. · 2015 · 21 · 33010.1002/psc.2719 ↗
14. Lauster · Angew. Chem., Int. Ed. · 2017 · 56 · 593110.1002/anie.201702005 ↗
15. Roma-Rodrigues · Int. J. Nanomed. · 2016 · 2633
16. Dey · Nat. Rev. Methods Primers · 2021 · 1 · 1310.1038/s43586-020-00009-8 ↗
17. Stephanopoulos · Chem · 2020 · 6 · 36410.1016/j.chempr.2020.01.012 ↗
18. Keller · Angew. Chem., Int. Ed. · 2020 · 59 · 1581810.1002/anie.201916390 ↗
19. Rothemund · Nature · 2006 · 440 · 29710.1038/nature04586 ↗
20. Ke · Science · 2012 · 338 · 117710.1126/science.1227268 ↗
21. Wei · Nature · 2012 · 485 · 62310.1038/nature11075 ↗
22. Möser · Int. J. Mol. Sci. · 2018 · 19 · 348210.3390/ijms19113482 ↗
23. Kwon · Nat. Chem. · 2020 · 12 · 2610.1038/s41557-019-0369-8 ↗
24. Kuzyk · Nature · 2012 · 483 · 31110.1038/nature10889 ↗
25. Shaw · Nat. Nanotechnol. · 2019 · 14 · 18410.1038/s41565-018-0336-3 ↗
26. Shaw · Nat. Methods · 2014 · 11 · 84110.1038/nmeth.3025 ↗
27. Douglas · Science · 2012 · 335 · 83110.1126/science.1214081 ↗
28. Liu · Nat. Mater. · 2021 · 20 · 42110.1038/s41563-020-0793-6 ↗
29. Lee · Sci. Adv. · 2022 · 8 · eadd018510.1126/sciadv.add0185 ↗
30. Lorenz · Adv. Mater. · 2018 · 30 · 170609210.1002/adma.201706092 ↗
31. Fuaad · Molecules · 2013 · 18 · 1314810.3390/molecules181113148 ↗
32. Tung · Bioconjugate Chem. · 2000 · 11 · 60510.1021/bc0000334 ↗
33. Jiang · J. Am. Chem. Soc. · 2017 · 139 · 1402510.1021/jacs.7b08087 ↗
34. Goodman · Science · 2005 · 310 · 166110.1126/science.1120367 ↗
35. MacCulloch · Org. Biomol. Chem. · 2019 · 17 · 166810.1039/C8OB02436G ↗
36. Winkler · Ther. Delivery · 2013 · 4 · 79110.4155/tde.13.47 ↗
37. Madani · J. Biophys. · 2011 · 2011 · 110.1155/2011/414729 ↗
38. Lindgren · Trends Pharmacol. Sci. · 2000 · 21 · 9910.1016/S0165-6147(00)01447-4 ↗
39. Snyder · Pharm. Res. · 2004 · 21 · 38910.1023/B:PHAM.0000019289.61978.f5 ↗
40. Koren · Trends Mol. Med. · 2012 · 18 · 38510.1016/j.molmed.2012.04.012 ↗
41. Ellington · Nature · 1990 · 346 · 81810.1038/346818a0 ↗
42. Ellington · Nature · 1992 · 355 · 85010.1038/355850a0 ↗
43. Lin · Proc. Natl. Acad. Sci. U. S. A. · 1995 · 92 · 1104410.1073/pnas.92.24.11044 ↗
44. Aviñó · Biochim. Biophys. Acta, Gen. Subj. · 2019 · 1863 · 161910.1016/j.bbagen.2019.06.014 ↗
45. Mela · Angew. Chem. · 2020 · 132 · 1279810.1002/ange.202002740 ↗
46. Agarwal · Angew. Chem., Int. Ed. · 2017 · 56 · 546010.1002/anie.201608873 ↗
47. Ponnuswamy · Nat. Commun. · 2017 · 8 · 1565410.1038/ncomms15654 ↗
48. Fasting · Angew. Chem., Int. Ed. · 2012 · 51 · 1047210.1002/anie.201201114 ↗
49. Vénien-Bryan · Acta Crystallogr., Sect. F: Struct. Biol. Commun. · 2017 · 73 · 17410.1107/S2053230X17003740 ↗
50. Nangreave · Biophys. J. · 2009 · 97 · 56310.1016/j.bpj.2009.05.013 ↗
51. Nangreave · J. Am. Chem. Soc. · 2011 · 133 · 449010.1021/ja1103298 ↗
52. Madsen · Chem. Rev. · 2019 · 119 · 638410.1021/acs.chemrev.8b00570 ↗
53. Diezmann · Biopolymers · 2010 · 94 · 39710.1002/bip.21440 ↗
54. Ede · Bioconjugate Chem. · 1994 · 5 · 37310.1021/bc00028a016 ↗
55. Nair · Chem. Mater. · 2014 · 26 · 72410.1021/cm402180t ↗
56. Zatsepin · Bioconjugate Chem. · 2002 · 13 · 82210.1021/bc020016+ ↗
57. Forget · Tetrahedron Lett. · 2001 · 42 · 917110.1016/S0040-4039(01)02017-2 ↗
58. King · Bioconjugate Chem. · 2014 · 25 · 82510.1021/bc500028d ↗
59. Nilsson · Org. Lett. · 2000 · 2 · 193910.1021/ol0060174 ↗
60. Saxon · Science · 2000 · 287 · 200710.1126/science.287.5460.2007 ↗
61. Mädler · J. Mass Spectrom. · 2009 · 44 · 69410.1002/jms.1544 ↗
62. Zubin · FEBS Lett. · 1999 · 456 · 5910.1016/S0014-5793(99)00921-7 ↗
63. Ameta · Org. Biomol. Chem. · 2014 · 12 · 470110.1039/C4OB00076E ↗
64. Hill · J. Org. Chem. · 2001 · 66 · 535210.1021/jo0100190 ↗
65. Steven · Org. Biomol. Chem. · 2008 · 6 · 378110.1039/b807843b ↗
66. Schoch · J. Am. Chem. Soc. · 2010 · 132 · 884610.1021/ja102871p ↗
67. Blackman · J. Am. Chem. Soc. · 2008 · 130 · 1351810.1021/ja8053805 ↗
68. Šečkutė · Nucleic Acids Res. · 2013 · 41 · e14810.1093/nar/gkt540 ↗
69. Rostovtsev · Angew. Chem., Int. Ed. · 2002 · 41 · 259610.1002/1521-3773(20020715)41:14<2596::AID-ANIE2596>3.0.CO;2-4 ↗
70. Hein · Angew. Chem., Int. Ed. · 2009 · 48 · 801810.1002/anie.200903558 ↗
71. Jewett · Chem. Soc. Rev. · 2010 · 39 · 127210.1039/b901970g ↗
72. Krell · Bioconjugate Chem. · 2020 · 31 · 99010.1021/acs.bioconjchem.0c00072 ↗
73. Patterson · ACS Chem. Biol. · 2014 · 9 · 59210.1021/cb400828a ↗
74. Zhou · J. Am. Chem. Soc. · 2013 · 135 · 1099410.1021/ja4066656 ↗
75. Campbell-Verduyn · Chem. Commun. · 2010 · 46 · 89810.1039/b919434g ↗
76. Brittain · ACS Catal. · 2016 · 6 · 362910.1021/acscatal.6b00996 ↗
77. Gong · Bioconjugate Chem. · 2016 · 27 · 21710.1021/acs.bioconjchem.5b00613 ↗
78. Stetsenko · J. Org. Chem. · 2000 · 65 · 490010.1021/jo000214z ↗
79. Thorand · J. Org. Chem. · 1998 · 63 · 855110.1021/jo9808021 ↗
80. Kent · Chem. Soc. Rev. · 2009 · 38 · 33810.1039/B700141J ↗
81. Soukchareun · Bioconjugate Chem. · 1998 · 9 · 46610.1021/bc980004h ↗
82. Lu · Bioconjugate Chem. · 2010 · 21 · 18710.1021/bc900158s ↗
83. Liu · Biochemistry · 1979 · 18 · 69010.1021/bi00571a022 ↗
84. G. T.Hermanson , in Bioconjugate Techniques , Elsevier , 2013 , pp. 229–25810.1016/B978-0-12-382239-0.00003-0 ↗
85. Cuatrecasas · Biochemistry · 1972 · 11 · 229110.1021/bi00762a013 ↗
86. Kalkhof · Anal. Bioanal. Chem. · 2008 · 392 · 30510.1007/s00216-008-2231-5 ↗
87. Lomant · J. Mol. Biol. · 1976 · 104 · 24310.1016/0022-2836(76)90011-5 ↗
88. Staros · Acc. Chem. Res. · 1988 · 21 · 43510.1021/ar00156a001 ↗
89. Gramlich · Angew. Chem., Int. Ed. · 2008 · 47 · 344210.1002/anie.200705664 ↗
90. Mahlapuu · Front. Cell. Infect. Microbiol. · 2016 · 6 · 19410.3389/fcimb.2016.00194 ↗
91. Liu · Nano Lett. · 2020 · 20 · 360210.1021/acs.nanolett.0c00529 ↗
92. Obuobi · J. Controlled Release · 2019 · 313 · 12010.1016/j.jconrel.2019.10.013 ↗
93. Obuobi · Nanoscale · 2020 · 12 · 1741110.1039/D0NR03095C ↗
94. Anastassacos · J. Am. Chem. Soc. · 2020 · 142 · 331110.1021/jacs.9b11698 ↗
95. Koga · Biomacromolecules · 2022 · 23 · 258610.1021/acs.biomac.2c00282 ↗
96. Bastings · Nano Lett. · 2018 · 18 · 355710.1021/acs.nanolett.8b00660 ↗
97. Wang · Proc. Natl. Acad. Sci. U. S. A. · 2020 · 117 · 633910.1073/pnas.1919749117 ↗
98. Ijäs · Nucleic Acids Res. · 2021 · 49 · 304810.1093/nar/gkab097 ↗
99. Liang · Angew. Chem., Int. Ed. · 2014 · 53 · 774510.1002/anie.201403236 ↗
100. Zanta · Proc. Natl. Acad. Sci. U. S. A. · 1999 · 96 · 9110.1073/pnas.96.1.91 ↗