Optimizing the selective recognition of protein isoforms through tuning of nanoparticle hydrophobicity.
We demonstrate that ligand hydrophobicity can be used to increase affinity and selectivity of binding between monolayer-protected cationic gold nanoparticles and β-lactoglobulin protein isoforms containing two amino acid mutations.
Department of Chemistry, University of Massachusetts at Amherst, Amherst, MA 01003, USA.|School of Chemical Engineering, East China University of Science and Technology, Shanghai 200237, China.
Kaimin
K
Chen
Department of Chemistry, University of Massachusetts at Amherst, Amherst, MA 01003, USA.
Subinoy
S
Rana
Department of Chemistry, University of Massachusetts at Amherst, Amherst, MA 01003, USA.
Daniel F
DF
Moyano
Department of Chemistry, University of Massachusetts at Amherst, Amherst, MA 01003, USA.
Yisheng
Y
Xu
School of Chemical Engineering, East China University of Science and Technology, Shanghai 200237, China.
Xuhong
X
Guo
Department of Chemistry, University of Massachusetts at Amherst, Amherst, MA 01003, USA.
Vincent M
VM
Rotello
D001665:Binding Sites; D006046:Gold / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D007782:Lactoglobulins / Q000737:chemistry* / Q000235:genetics / Q000648:ultrastructure*; D008422:Materials Testing; D053768:Metal Nanoparticles / Q000737:chemistry* / Q000648:ultrastructure; D016297:Mutagenesis, Site-Directed; D053761:Nanocomposites / Q000737:chemistry* / Q000648:ultrastructure; D010316:Particle Size; D011485:Protein Binding; D020033:Protein Isoforms / Q000737:chemistry / Q000648:ultrastructure; D013329:Structure-Activity Relationship
D007782:Lactoglobulins; D020033:Protein Isoforms; D006046:Gold