Probing the protein-nanoparticle interface: The role of aromatic substitution pattern on affinity

EKMEKÇİ Z., Saha K., Moyano D. F., Tonga G. Y., Wang H., Mout R., ...Daha Fazla

Supramolecular Chemistry, cilt.27, ss.123-126, 2015 (SCI-Expanded, Scopus) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 27
  • Basım Tarihi: 2015
  • Doi Numarası: 10.1080/10610278.2014.914627
  • Dergi Adı: Supramolecular Chemistry
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.123-126
  • Anahtar Kelimeler: aromatic substitution, gold nanoparticles, nanoparticle-protein affinity
  • Isparta Uygulamalı Bilimler Üniversitesi Adresli: Hayır

Özet

A new class of cationic gold nanoparticles (NPs) has been synthesised bearing benzyl moieties featuring-NO2 and -OMe groups to investigate the regioisomeric control of aromatic NP-protein recognition. In general, NPs bearing electron-withdrawing groups demonstrated higher binding affinities towards green fluorescent protein (GFP) than NPs bearing electron-donating groups. Significantly, a ~7.5- and ~4.3-fold increase in binding with GFP was observed for -NO2 groups in meta-position and para-position, respectively, while ortho-substitution showed binding similar to the unsubstituted ring. These findings demonstrated that the NP-protein interaction can be controlled by tuning the spatial orientation and the relative electronic properties of the aromatic substituents. This improved biomolecular recognition provides opportunities for enhanced biosensing and functional protein delivery to the cells.