Peptide-directed binding of quantum dots to integrins in human fibroblast.
There is currently a major international effort aimed at integrating semiconductor nanostructures with biological structures. This paper reports the use of peptide sequences with certain motifs like artinine-glycine-aspartic acid (RGD) and leucine-aspartic acid-valine (LDV) to functionalize zinc sulfide (ZnS)-capped cadmiun selenide (CdSe) quantum dots, so that the quantum dot-peptide complexes selectively bind to integrins on HT1080 human fibrosarcoma cells membrane. In this way, an interface between semiconductor nanocrystals and subcellular components was achieved, and the distribution pattern of RGD and LDV receptors on HT1080 cell membranes is revealed. These findings point the way to using a wide class of peptide-functionalized semiconductor quantum dots for the study of cellular processes involving integrins.
Department of Bioengineering, University of Illinois, Chicago, IL 60607, USA.
Peng
P
Shi
Hongfeng
H
Chen
Michael R
MR
Cho
Michael A
MA
Stroscio
D001665:Binding Sites; D002460:Cell Line; D006801:Humans; D007118:Immunoassay / Q000379:methods*; D016023:Integrins / Q000378:metabolism*; D008856:Microscopy, Fluorescence / Q000379:methods*; D010455:Peptides / Q000737:chemistry*; D011485:Protein Binding; D045663:Quantum Dots
D016023:Integrins; D010455:Peptides