journal article·2013-11-26

Reversible Chirality Control in Peptide-Functionalized Gold Nanoparticles

Edoardo Longo, Andrea Orlandin, Fabrizio Mancin, Paolo Scrimin, Alessandro Moretto

ACS Nano· Volume 7· Issue 11
Publisher page

Abstract

We report the induction of chiroptical properties in 2 nm diameter gold nanoparticles passivated with short peptides characterized by the Aib-l-Ala repetition in their sequence. The nanoparticles present relevant ECD signals in the 300-650 nm wavelength region, corresponding to the gold nanoparticle's quantized electronic structure. Although the only chiral amino acid present in the peptide sequences is l-Ala, the particles show mirror image spectra like those of enantiomers according to the number of amino acids in the main chain (odd or even). Such a behavior appears to be strongly influenced by the secondary structure assumed by the peptides when passivating the nanoparticles and vanishes when the sequence is long enough to assume a 310-helix conformation. Moreover, chirality control is a reversible process and can be deactivated or reactivated by increasing or decreasing the temperature.
Source: openalex_inverted_index · Quality: baseline

Research context

OpenAlex topics: Nanocluster Synthesis and Applications · Supramolecular Self-Assembly in Materials · Gold and Silver Nanoparticles Synthesis and Applications

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

Department of Chemical Sciences, University of Padova, Via Marzolo 1, 35131 Padova, Italy

References (33)

Show source-provided references
1. Pasquato L. · J. Mater. Chem. · 2004 · 14 · 348110.1039/b410476e ↗
2. Ojea-Jimenez I. · J. Am. Chem. Soc. · 2009 · 131 · 1332010.1021/ja902894s ↗
3. Duchesne L. · ChemBioChem · 2009 · 9 · 212710.1002/cbic.200800326 ↗
4. Levy R. · ChemBioChem · 2006 · 7 · 114110.1002/cbic.200600129 ↗
5. Pengo P. · J. Am. Chem. Soc. · 2005 · 127 · 161610.1021/ja043547c ↗
6. Pengo P. · Angew. Chem., Int. Ed. · 2007 · 46 · 40010.1002/anie.200602581 ↗
7. Free P. · Chem. Commun. · 2009 · 500910.1039/b910657j ↗
8. Zaramella D. · J. Am. Chem. Soc. · 2012 · 134 · 839610.1021/ja302754h ↗
9. Guarise C. · Proc. Natl. Acad. Sci. U.S.A. · 2006 · 103 · 397810.1073/pnas.0509372103 ↗
10. Bonomi R. · Angew. Chem., Int. Ed. · 2011 · 50 · 230710.1002/anie.201007389 ↗
11. Raha S. · WIREs Nanomed. Nanobiotechnol. · 2011 · 3 · 26910.1002/wnan.121 ↗
12. Huang X. · ACS Nano · 2010 · 4 · 588710.1021/nn102055s ↗
13. Ghosh P. S. · ACS Nano · 2008 · 2 · 221310.1021/nn800507t ↗
14. Yan X. · ACS Nano · 2012 · 6 · 11110.1021/nn202939s ↗
15. Schaaff T. G. · J. Phys. Chem. B · 1998 · 102 · 1064310.1021/jp9830528 ↗
16. George J. · J. Am. Chem. Soc. · 2010 · 132 · 250210.1021/ja908574j ↗
17. Shukla N. · J. Am. Chem. Soc. · 2010 · 132 · 857510.1021/ja908219h ↗
18. Rezanka P. · Colloids Surf., A · 2011 · 374 · 7710.1016/j.colsurfa.2010.11.015 ↗
19. Häkkinen H. · Nat. Chem. · 2012 · 4 · 44310.1038/nchem.1352 ↗
20. Gautier C. · ChemPhysChem · 2009 · 10 · 48310.1002/cphc.200800709 ↗
21. Jadzinsky P. D. · Science · 2007 · 318 · 43010.1126/science.1148624 ↗
22. Rio-Echevarria I. · J. Am. Chem. Soc. · 2011 · 133 · 810.1021/ja107588q ↗
23. Schade M. · Nano Lett. · 2010 · 11 · 305710.1021/nl101580w ↗
24. Longo E. · Chirality · 2011 · 23 · 75610.1002/chir.20986 ↗
25. Hostetler M. J. · Langmuir · 1998 · 14 · 1710.1021/la970588w ↗
26. Fabris L. · J. Am. Chem. Soc. · 2006 · 128 · 32610.1021/ja0560581 ↗
27. Barth A. · Rev. Biophys. · 2002 · 35 · 36910.1017/S0033583502003815 ↗
28. Arrondo J. L. R. · Prog. Biophys. Mol. Biol. · 1993 · 59 · 2310.1016/0079-6107(93)90006-6 ↗
29. Shaw C. P. · ACS Nano · 2012 · 6 · 141610.1021/nn204214x ↗
30. Dolamic I. · Nat. Commun. · 2012 · 3 · 79810.1038/ncomms1802 ↗
31. Qian H. · J. Am. Chem. Soc. · 2010 · 132 · 828010.1021/ja103592z ↗
32. Knoppe S. · Angew. Chem., Int. Ed. · 2012 · 51 · 758910.1002/anie.201202369 ↗
33. Knoppe S. · J. Am. Chem. Soc. · 2012 · 134 · 1311410.1021/ja3053865 ↗