Ricardo Capone

Ricardo Capone 

Assistant Project Scientist

Contact Information

Assistant Project Scientist

Email:ricardo.capone@gmail.com

Mailing Address:
9500 Gilman Drive #0649
La Jolla, CA  92093-0649


Ricardo Capone earned his BA/MS in biology and molecular genetics from the University of Milan, Italy, and his PhD in biological chemistry from Hebrew University of Jerusalem in Israel. In the US he was a postdoctoral fellow at the University Michigan in the Department of Biologic and Materials Sciences as well as the Department of Biomeidcal Engineering.

In 2008 he joined the University of Chicago and in 2010 UC San Diego, first in the department of Bioengineering and in 2012 the Department of Neurosciences.

Dr. Capone's research studies currently focus on γ-secretase activity assays and modulation of its proteolytic activity. The enzyme γ-secretase is responsible for the last proteolytic step that generates amyloid β peptides, eventually forming β-amyloid plaques. Amyloid plaques are found in several neurodegenerative diseases, such as in older persons with Down syndrome, in Alzheimer’s disease and other age-related dementias.

The ultimate goal of this research is to find ways reduce the excess production of Aβ so that the normal cellular mechanisms of protein clearance can maintain the normal required levels of Aβ peptides.

See more about research at our Down Syndrome Center for Research and Treatment.

Peer-reviewed Publications

Capone R*, Jang H*, Kotler S.A, Connelly L, Teran Arce F, Ramachandran S, Kagan B.L, Nussinov R, Lal R. (2012) All-D-Enantiomer of β-Amyloid Peptide Forms Ion Channels in Lipid Bilayers J. Chem. Theory Comput. 8 (3): 1143-1152

Capone R*, Jang H*, Kotler SA*, Nussinov R, Lal R. (2012) Probing Structural Features of Alzheimer’s β-Amyloid Pores in Bilayers Using Site-Specific Amino Acid Substitutions. Biochemistry 51(3) 776-85

Connelly L, Teran Arce F, Jang H, Capone R, Kotler S.A, Ramachandran S, Kagan B.L, Nussinov R, Lal R. (2012) Atomic Force Microscopy and MD Simulations Reveal Pore-Like
Structures of All-D-Enantiomer of Alzheimer’s β-Amyloid Peptide: Relevance to the Ion Channel Mechanism of AD Pathology J. Phys. Chem. B. 116(5), 1728-35

Kagan BL, Jang H, Capone R, Teran Arce F, Ramachandran S, Lal R., Nussinov R. (2012) Antimicrobial Properties of Amyloid Peptides Mol. Pharm. 9(4): 708-717 (Review)

Allen1 MJ*, Lacroix JJ*, Ramachandran S*, Capone R, Whitlock JL, Ghadge GD, Arnsdorf MF, Roos RP, Lal R. (2012) Mutant SOD1 forms ion channel: implications for ALS pathophysiology. Neurobiol Dis. 45 (3): 831-838
(Selected for cover picture)

Jang H, Teran Arce F, Mustata M, Ramachandran S, Capone R, Nussinov R, Lal R. (2011) Antimicrobial Protegrin-1 Forms Amyloid-like Fibrils with Rapid Kinetics Suggesting a Functional Link. Biophys J. 100 (7):1775-83
(Commented on Biophys J. 100(7):1597-8)

Jang H, Teran Arce F, Ramachandran S, Capone R, Lal R, Nussinov R. (2010) β-Barrel Topology of Alzheimer's β-Amyloid Ion Channels. J Mol Biol. 404(5), 917-34

Jang H, Teran Arce F, Ramachandran S, Capone R, Lal R, Nussinov R (2010) Structural convergence among diverse, toxic beta-sheet ion channels. J. Phys. Chem. B. 114(29), 9445-51

Godovikova V, Wang HT, Goetting-Minesky MP, Ning Y, Capone RF, Slater CK, Fenno JC. (2010) Treponema denticola PrcB is required for expression and activity of the PrcA-PrtP (dentilisin) complex. J. Bacteriol. 192 (13):3337-44

Capone R*, Mustata M*, Jang H*, Teran Arce F, Nussinov R, Lal R. (2010) Antimicrobial Protegrin-1 (PG-1) Forms Ion Channels: MD Simulation, AFM, and Electrical Conductance Studies. Biophys J. 98 (11), 2644-52
*equally contributed

Jang H*, Teran Arce F*, Ramachandran S*, Capone R, Azimova R, Kagan BL, Nussinov R, Lal R. (2010) Truncated β-amyloid peptide channels provide an alternative mechanism for Alzheimer’s Disease and Down syndrome Proc. Natl. Acad. Sci. USA 107 (14), 6538-43

Macrae MX, Blake S, Jiang X, Capone R, Estes DJ, Mayer M, Yang J. (2009) A Semi-Synthetic Ion Channel Platform for Detection of Phosphatase and Protease Activity. ACS Nano 3(11), 3567-3580

Jang H, Teran Arce F, Capone R, Ramachandran S, Lal R, Nussinov R. (2009) Toxic Alzheimer Ion Channels Present Loose Mobile Subunits Organization in the Membrane in Contrast to Tightly Interacting Helical Gated Channels Biophys J. 97 (11), 3029-3037

Capone R, Garcia Quiroz F, Prangkio P, Saluja I, Sauer A. M., Bautista M.R., Turner R. S., Yang J. and M. Mayer (2009). Amyloid-β Induced Ion Flux in Artificial Lipid Bilayers and in Neuronal Cells: Resolving a Controversy. Neurotox. Res. 16(1), 1-13.

Mustata M*, Capone R*, Jang H*, Teran Arce F, Ramachandran S, Lal R, Nussinov R. (2009) The K3 fragment of amyloidogenic β2-microglobulin forms ion channel: Implication for Dialysis Related Amyloidosis. J. Am. Chem. Soc. 131 (41), 14938-14945
*equally contributed

Horger K, Estes D, Capone R, and M. Mayer (2009) Films of Agarose Enable Rapid Formation of Giant Liposomes in Solutions of Physiological Ionic Strength. J. Am. Chem. Soc., 131 (5), 1810-1819

Blake S, Capone R, Mayer M, and J. Yang (2008). Chemically Reactive Derivatives of Gramicidin A for the Developing of Ion Channel-Based Nanoprobes. Bioconj Chem 19(8), 1614-1624

Capone R, Wang H.T, Ning Y, Sweier D.G, Lopatin D.E. and J.C. Fenno. (2008). Human Serum Antibodies Recognize Treponema denticola Msp and PrtP Protease Complex Proteins. Oral Microbiol. Immunol. 23, 165-169

Capone R, Blake S, Rincón-Restrepo M, Yang J, and M. Mayer (2007) Designing Nanosensors Based on Charged Derivatives of Gramicidin A. J. Am. Chem. Soc., 129 (31), 9737 -9745.

Capone R.F; Ning Y; Pakulis N; Alhazzazi T, and JC Fenno. (2007). Characterization of Treponema denticola pyrF Encoding Orotidine-5 '-Monophosphate Decarboxylase. FEMS Microbiol. Lett. 268 (2): 261-267.

Nadav A, Diskin R, Avitzour M, Capone R, Livnah O and D Engelberg (2007). Hyperactive Variants of p38α Induce, Whereas Hyperactive Variants of p38α Suppress AP-1-mediated Transcription. J. Biol. Chem. 282(1):91-9.

Diskin R, Askari N, Capone R, Engelberg D, and O. Livnah (2004). Active Mutants of the Human p38α Mitogen-activated Protein Kinase. J Biol. Chem. 279(45):47040-9.

Capone R, Tiwari B.S, and A. Levine (2004). Rapid Transmission of Oxidative and Nitrosative Stress Signals from Roots to Shoots in Arabidopsis. Plant Physiol. Biochem. 42(5):425-8.

Bell M, Capone R, Pashtan I, Levitzki A, and D. Engelberg. (2001). Isolation of Hyperactive Mutants of the MAPK p38/Hog1 that are Independent of MAPKK Activation. J. Biol. Chem. 276(27): 25351-8.

Pozzi C, Faccioli P, Terzi V, Stanca AM, Cerioli S, Castiglioni P, Fink R, Capone R, Muller KJ, Bossinger G, Rohde W, and F. Salamini. (2000). Genetic of Mutations Affecting the Development of Barley Floral Bract. Genetics 154 (3): 1335-46.

Kleinberger-Doron N, Shelah N, Capone R, Gazit A, and Levitzki A. (1998). Inhibition of Cdk2 Activation by Selected Tryrphostins Causes Cell Cycle Arrest at Late G1 and S Phase. Exp. Cell Res. 241(2): 340-51

Foiani M, Nadjar-Boger E, Capone R, Sagee S, Hashimshoni T, and Kassir Y. (1996). A Meiosis-Specific Protein Kinase, Ime2, Is Required for the Correct Timing of DNA Replication and for Spore Formation in Yeast Meiosis. Mol. Gen. Genet. 253 (3): 278-288.