Abstract
Results of our study of structural properties of the nanoscale integrated semiconductor quantum dots such as CdS and ZnS-capped CdSe, conjugated with biomolecules such as short peptides and cells are presented. Nanoscale functionalization of semiconductor quantum dots with biomedical structures is promising for many applications and novel studies of intrinsic properties of both constituent systems. We study CdS semiconductor quantum dots functionalized with peptides composed of the following amino acid chains: CGGGRGDS, CGGGRVDS, CGGIKVAV, and CGGGLDV, where R is arginine, D is aspartic acid, S is serine, V is valine, K is lysine and L is Levine. As will be seen the cysteine (C) amino acid links to CdS semiconductor quantum dots via the thiol link. Furthermore, the GGG sequences of glycine (G) amino acids provide a spacer in the amino acid chain. At the same time the RGDS, RVDS, IKAV, and LDV sequences have selective bonding affinities to specialized transmembrane cellular structures known as integrins of neurons and MDA-MB-435 cancer cells, respectively. Since protein hydration is known to be a key factor affecting protein energy balance, we also studied a role that water and other bioenvironments may play in stability, surface properties, dynamical and structural characteristics of these systems. We found also the roles that the quantum confinement and functionalizing in the biomedical environments play in altering and determining the electronic, optical, and vibrational properties of these nanostructures as well as demonstrated the effectiveness to use the semiconductor quantum dots as integrin sensitive biotags.
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