Carbon nanotubes are functionalized by bovine serum albumin (BSA) proteins via diimide-activated amidation under ambient conditions. The nanotube-BSA conjugates thus obtained are highly water-soluble, forming dark-colored aqueous solutions. Results from characterizations using atomic force microscopy (AFM), thermal gravimetric analysis, Raman, and gel electrophoresis show that the conjugate samples indeed contain both carbon nanotubes and BSA proteins and that the protein species are intimately associated with the nanotubes. Bioactivities of the nanotube-bound proteins are evaluated using the total protein micro-determination assay (the modified Lowry procedure). The results show that the overwhelming majority (∼90%) of the protein species in the nanotube-BSA conjugates remain bioactive.

X-ray analysis has revealed that 4,4′-bipyridine, 1,2-bis(4-pyridyl)ethylene, and hexamethylenetetramine form donor-acceptor complexes with 1,4-diiodobenzene, 1,4-diiodotetrafluorobenzene, and tetraiodoethylene in which the N‚‚‚I distance is longer than that for the corresponding I 2 complexes. As opposed to the corresponding I 2 complexes that are molecular adducts, these complexes have extended structures and longer N‚‚‚I distances. Steric and electronic effects influence the strength of the N‚‚‚I interaction and the crystal packing. An additional complex of 1,2-bis(4-pyridyl)ethane and 1,4-dibromotetrafluorobenzene has also been investigated for comparison of N‚‚‚I and N‚‚‚Br interactions.