Publications

Yang, Z. P., and A. Chilkoti. “Light-activated affinity micropatterning of proteins.” Annual International Conference of the IEEE Engineering in Medicine and Biology Proceedings 2 (December 1, 1999): 738.

Meyer, D. E., G. Kong, M. Dewhirst, and A. Chilkoti. “Genetically-engineered polypeptide carrier for thermal targeting of therapeutics.” Annual International Conference of the IEEE Engineering in Medicine and Biology Proceedings 2 (December 1, 1999): 1289.

Stayton, P. S., S. Freitag, L. A. Klumb, A. Chilkoti, V. Chu, J. E. Penzotti, R. To, et al. “Streptavidin-biotin binding energetics.” Biomolecular Engineering 16, no. 1–4 (December 1999): 39–44. https://doi.org/10.1016/s1050-3862(99)00042-x.

Freitag, S., I. Le Trong, L. A. Klumb, V. Chu, A. Chilkoti, P. S. Stayton, and R. E. Stenkamp. “X-ray crystallographic studies of streptavidin mutants binding to biotin.” Biomolecular Engineering 16, no. 1–4 (December 1999): 13–19. https://doi.org/10.1016/s1050-3862(99)00048-0.

Meyer, D. E., and A. Chilkoti. “Purification of recombinant proteins by fusion with thermally-responsive polypeptides.” Nat Biotechnol 17, no. 11 (November 1999): 1112–15. https://doi.org/10.1038/15100.

Meyer, D. E., and A. Chilkoti. “Polypeptide fusion tag for thermal purification of recombinant proteins.” ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY 217 (March 21, 1999): U177–U177.

Freitag, S., I. Le Trong, A. Chilkoti, L. A. Klumb, P. S. Stayton, and R. E. Stenkamp. “Structural studies of binding site tryptophan mutants in the high-affinity streptavidin-biotin complex.” Journal of Molecular Biology 279, no. 1 (May 1998): 211–21. https://doi.org/10.1006/jmbi.1998.1735.

Hoffman, A. S., P. S. Stayton, T. Shimoboji, G. Chen, Z. Ding, A. Chilkoti, C. Long, et al. “Conjugates of Stimuli-Responsive Polymers and Biomolecules: Random and Site-Specific Conjugates of Temperature-Sensitive Polymers and Proteins.” Macromolecular Symposia 118 (January 1, 1997): 553–62. https://doi.org/10.1002/masy.19971180173.

Shimoboji, T., P. S. Stayton, C. Long, A. Chilkoti, G. Chen, J. M. Harris, and A. S. Hoffman. “Site-specific conjugation of a temperature-sensitive polymer to a genetically-engineered protein.” Transactions of the Annual Meeting of the Society for Biomaterials in Conjunction with the International Biomaterials Symposium 1 (December 1, 1996): 897.

Frey, W., W. R. Schief, D. W. Pack, C. T. Chen, A. Chilkoti, P. Stayton, V. Vogel, and F. H. Arnold. “Two-dimensional protein crystallization via metal-ion coordination by naturally occurring surface histidines.” Proceedings of the National Academy of Sciences of the United States of America 93, no. 10 (May 1996): 4937–41. https://doi.org/10.1073/pnas.93.10.4937.

Chilkoti, A., T. Boland, B. D. Ratner, and P. S. Stayton. “The relationship between ligand-binding thermodynamics and protein-ligand interaction forces measured by atomic force microscopy.” Biophysical Journal 69, no. 5 (November 1995): 2125–30. https://doi.org/10.1016/s0006-3495(95)80083-4.

Chilkoti, A., B. L. Schwartz, R. D. Smith, C. J. Long, and P. S. Stayton. “Engineered chimeric streptavidin tetramers as novel tools for bioseparations and drug delivery.” Bio/Technology (Nature Publishing Company) 13, no. 11 (November 1995): 1198–1204. https://doi.org/10.1038/nbt1195-1198.

Stayton, P. S., T. Shimoboji, C. Long, A. Chilkoti, G. Chen, J. M. Harris, and A. S. Hoffman. “Control of protein-ligand recognition using a stimuli-responsive polymer.” Nature 378, no. 6556 (November 1995): 472–74. https://doi.org/10.1038/378472a0.

Chilkoti, A., A. E. Schmierer, V. H. Pérez-Luna, and B. D. Ratner. “Investigating the relationship between surface chemistry and endothelial cell growth: partial least-squares regression of the static secondary ion mass spectra of oxygen-containing plasma-deposited films.” Analytical Chemistry 67, no. 17 (September 1995): 2883–91. https://doi.org/10.1021/ac00113a024.

Schwartz, B. L., J. E. Bruce, G. A. Anderson, S. A. Hofstadler, A. L. Rockwood, R. D. Smith, A. Chilkoti, and P. S. Stayton. “Dissociation of tetrameric ions of noncovalent streptavidin complexes formed by electrospray ionization.” Journal of the American Society for Mass Spectrometry 6, no. 6 (June 1995): 459–65. https://doi.org/10.1016/1044-0305(95)00191-f.

Chilkoti, A., P. H. Tan, and P. S. Stayton. “Site-directed mutagenesis studies of the high-affinity streptavidin-biotin complex: contributions of tryptophan residues 79, 108, and 120.” Proceedings of the National Academy of Sciences of the United States of America 92, no. 5 (February 1995): 1754–58. https://doi.org/10.1073/pnas.92.5.1754.

Chilkoti, A., and P. S. Stayton. “Molecular Origins of the Slow Streptavidin—Biotin Dissociation Kinetics.” Journal of the American Chemical Society 117, no. 43 (January 1, 1995): 10622–28. https://doi.org/10.1021/ja00148a003.

Schwartz, B. L., D. C. Gale, R. D. Smith, A. Chilkoti, and P. S. Stayton. “Investigation of non‐covalent ligand binding to the intact streptavidin tetramer by electrospray ionization mass spectrometry.” Journal of Mass Spectrometry 30, no. 8 (January 1, 1995): 1095–1102. https://doi.org/10.1002/jms.1190300806.

Chilkoti, A., G. Chen, P. S. Stayton, and A. S. Hoffman. “Site-specific conjugation of a temperature-sensitive polymer to a genetically-engineered protein.” Bioconjugate Chemistry 5, no. 6 (November 1994): 504–7. https://doi.org/10.1021/bc00030a004.

Chilkoti, A., B. D. Ratner, and D. Briggs. “Static secondary ion mass spectrometric investigation of the surface chemistry of organic plasma-deposited films created from oxygen-containing precursors. 3. Multivariate statistical modeling.” Analytical Chemistry 65, no. 13 (July 1993): 1736–45. https://doi.org/10.1021/ac00061a017.

Chilkoti, A., G. P. Lopez, B. D. Ratner, M. J. Hearn, and D. Briggs. “Analysis of Polymer Surfaces by SIMS. 16. Investigation of Surface Cross-Linking in Polymer Gels of 2-Hydroxyethyl Methacrylate.” Macromolecules 26, no. 18 (January 1, 1993): 4825–32. https://doi.org/10.1021/ma00070a016.

Chilkoti, A., and B. D. Ratner. “X-ray Photoelectron Spectroscopy of Iodine-Doped Nonconjugated Polymers.” Chemistry of Materials 5, no. 6 (January 1, 1993): 786–92. https://doi.org/10.1021/cm00030a012.

Ratner, B. D., B. J. Tyler, and A. Chilkoti. “Analysis of biomedical polymer surfaces: polyurethanes and plasma-deposited thin films.” Clinical Materials 13, no. 1–4 (January 1993): 71–84. https://doi.org/10.1016/0267-6605(93)90093-m.

Stayton, P. S., A. Chilkoti, C. J. Long, D. K. Pettit, P. H. S. Tan, G. Chen, and A. S. Hoffman. “Engineered proteins for biomaterials.” Materials Research Society Symposium Proceedings 292 (January 1, 1993): 77–82.

López, G. P., A. Chilkoti, D. Briggs, and B. D. Ratner. “Substrate temperature effects on film chemistry in plasma deposition of organics. III. Analysis by static secondary ion mass spectrometry.” Journal of Polymer Science Part A Polymer Chemistry 30, no. 11 (January 1, 1992): 2427–41. https://doi.org/10.1002/pola.1992.080301117.