Associate Professor, Department of Chemistry and Chemical Biology
Rensselaer Polytechnic Institute

Education:
Ph.D., Chemistry, Texas A&M University, 1993
B.S., Chemistry, Summa Cum Laude, the University of Puerto Rico at Mayagüez, 1988

Career Highlights:
After serving as a postdoctoral associate and then as a National Science Foundation (NSF) Fellow at the Fox Chase Cancer Center in Philadelphia, Colón joined the Rensselaer faculty in 1997. He was promoted to associate professor in 2004.

Colón’s many honors and awards include a Rensselaer Early Career Award in 2002, an NSF Presidential Early Career Award for Scientists and Engineers (PECASE) in 2001, an NSF Faculty Early Career Development (CAREER) Award in 2000, and a Research Corporation Innovation Award in 1999. He also has earned the American Heart Association’s Scientist Development Award and a New Faculty Award from the Camille and Henry Dreyfus Foundation.

Research Areas:
Colón’s laboratory is interested in understanding the chemical and physical principles of molecular recognition by which the amino acid sequence of a protein leads to its folding, oligomerization, and aggregation. Substantial evidence obtained in recent years suggests that the molecular basis of a number of diseases is intimately related to protein misfolding and aggregation. Among these so-called “conformational disorders” is a family of diseases generically known as amyloid diseases, which include Alzheimer’s, Parkinson’s, Huntington, and Prion diseases.

Colón’s research focuses on two general areas: the role of structural intermediate(s) in the mechanism of protein folding, misfolding, and oligomerization; and understanding the molecular basis for protein stability against misfolding and degradation. His group’s long-term goal is the design of therapeutic agents for misfolding diseases and the design of long-lived proteins for industrial purposes.

In particular, biophysical studies on the proteins serum amyloid A (SAA) and Cu/Zn superoxide dismutase (SOD) are being pursued to understand the role of defective folding or assembly of these proteins in the pathogenesis of reactive amyloidosis and amyotrophic lateral sclerosis (Lou Gehrig’s disease), respectively. In a separate project, methodology is being developed to allow the identification and generation of long-lived kinetically stable proteins.

Selected Publications:
M.D. de Beus, J. Chung, and W. Colón, “Modification of Cysteine 111 in Cu/Zn Superoxide Dismutase Results in Altered Spectroscopic and Biophysical Properties,” Protein Science, 13, (5), 1347-1355, (2004).

L. Wang and W. Colón, “The Interaction Between Apolipoprotein Serum Amyloid A and High-Density Lipoprotein, Biochemical and Biophysical Research Communications, 317, 157-161, (2004).

S.A. Boswell, J. Mathew, M. Beach, R. Osuna, and W. Colón, “The Variable Contributions of Tyrosine Residues to the Structural and Spectroscopic Properties of the Factor for Inversion Stimulation,” Biochemistry, 43, (10), 2964-2977, (2004).

J. Chung, H. Yang, M.D. de Beus, C.Y. Ryu, H. Cho, and W. Colón, “Cu/Zn Superoxide Dismutase Can Form Pore-Like Structures,” Biochemical and Biophysical Research Communications, 312, (4), 873-876, (2003).

L. Wang, H.A. Lashuel, T. Walz, and W. Colón, “Murine Apolipoprotein Serum Amyloid A in Solution Forms A Hexamer Containing A Central Channel,” Proceedings of the National Academy of Sciences of the United States of America, 99, (25), 15947-15952, (2002).

S.A. Hobart, D. Meinhold, R. Osuna, and W. Colón, “From Two-State to Three-State: Effect of P61A Mutation on the Dynamics and Stability of the Factor for Inversion Stimulation Results in an Altered Equilibrium Denaturation Mechanism,” Biochemistry, 41, (46), 13744-13754, (2002).

W. Colón, “Solving the Protein Folding Problem,” Chemical & Engineering News, March 26, 2001, p. 225.

H. Roder and W. Colón, “Kinetic Role of Early Intermediates in Protein Folding,” Current Opinion in Structural Biology, 7, (1), 15-28, (1997).

W. Colón and H. Roder, “Kinetic Intermediates in the Formation of the Cytochrome c Molten Globule,” Nature Structural Biology, 3, 1019-1025, (1996).

W. Colón, G.E. Elöve, L.P. Wakem, F. Sherman, and H. Roder, “Side Chain Packing of the N- and C- Terminal Helices Plays a Critical Role in the Kinetics of Cytochrome c Folding,” Biochemistry, 35, (17), 5538-5549, (1996).

S.L. McCutchen, Z. Lai, G.J. Miroy, J.W. Kelly, and W. Colón, “Comparison of Lethal and Nonlethal Transthyretin Variants and Their Relationship to Amyloid Disease,” Biochemistry, 34, (41), 13527-13536, (1995).

W. Colón and J.W. Kelly, “Partial Denaturation of Transthyretin is Sufficient for Amyloid Fibril Formation In Vitro,” Biochemistry, 31, (36), 8654-8660, (1992).

Contact Information:
Wilfredo Colón
(518) 276-2515
colonw@rpi.edu
http://www.rpi.edu/dept/chem/chem_faculty/profiles/colon.html