Richard Chamberlin
Joint appointment, Chemistry
School of Physical Sciences
School of Physical Sciences
Professor and Chair, Department of Pharmaceutical Sciences
Joint Appointment, Pharmacology
School of Medicine
School of Medicine
PH.D., University of California, San Diego, 1978
OTH
OTH
University of California, Irvine
4206 Natural Sci. I & 147 Biol. Sci. Admin.
Mail Code: 2025
Irvine, CA 92697
4206 Natural Sci. I & 147 Biol. Sci. Admin.
Mail Code: 2025
Irvine, CA 92697
Research Interests
Organic Synthesis, Chemical Biology
Websites
Academic Distinctions
Fellow, American Association for the Advancement of Science
Eli Lilly Grantee
UCI Physical Sciences, Distinguished Teaching Award
NIH Career Development Award in neuroscience
Eli Lilly Grantee
UCI Physical Sciences, Distinguished Teaching Award
NIH Career Development Award in neuroscience
Appointments
1978-80, NIH Postdoctoral Fellow, Harvard University
Joined UCI faculty in 1980
Joined UCI faculty in 1980
Research Abstract
Chemical synthesis is the central tool in our general objective of controlling the biological activities of important target proteins with new small molecule ligands. Current objectives include neurotransmitter receptors, serine-threonine phosphatases, potassium channels, HIV integrase, and the tumor suppressor p53.
The overall goal of one project is to understand at a molecular level the interactions between the membrane receptors that mediate excitatory neurotransmission and the endogenous ligand that activates them, glutamic acid. The traditional division of ionotropic glutamate receptors (iGluRs) into three classes (NMDA, AMPA, KA) with distinct pharmacological properties is rapidly becoming obsolete with the recent characterization of multiple sub-types of each class, each likely controlling different functions. Our current goal is to develop sub-type selective ligands that will clearly delineate the distinct functions of each iGluR sub-type. Employing ligand design in conjunction combinatorial library synthesis (often based on structures of natural toxins that interact with iGluR receptors), with these studies may not only lead to a better understanding of such important processes as learning and memory, but also provide new details on mechanisms of brain damage in disorders such as stroke, epilepsy, and Alzheimer's disease.
A second area of interest is the design and synthesis of small molecules that modulate the activity of the important serine-threonine protein phosphatases PP1 and PP2A. Inhibitors such as the naturally occurring toxins okadaic acid, microcystin, and tautomycin have been the only available small molecule probes used by cell biologists to study the respective roles of PP1 and PP2A in cellular signaling pathways. Using these natural products as "lead" compounds, we are designing and synthesizing simplified analogues with improved selectivity or other valuable properties. For example, we have recently shown that highly truncated versions of microcystin and tautomycin retain nanomolar activities (albeit at significantly reduced levels compared to the parent toxins) and thus provide relatively easy-to-prepare scaffolds for exciting new studies of in vivo imaging of phosphatase trafficking via fluorescently labeled versions of the truncated compounds.
Applying a similar general strategy, we are designing new compounds based on the structure of the natural terpenoid correolide, which has recently been reported to be a potent blocker of certain types of potassium channels that are particularly abundant in the T-cells of the immune system. The goal is to discover a more selective blocker, preferably with a considerably simpler structure, that would serve as a lead compound for a new type of immunosuppressant drug.
Finally, we are working on several collaborative projects with fellow UCI Comprehensive Cancer Center members to develop new types of anti-tumor compounds. Many labs have made substantial progress in the past several years in developing effective chemotherapeutic agents for the treatment of HIV infection, but there remains a substantial demand for new strategies. Our approach is to employ computational ligand-based design in conjunction with combinatorial library synthesis to develop new HIV Integrase (IN) inhibitors based on the natural product IN inhibitor chicoric acid. We are also participants in a separate exciting collaboration that targets the tumor suppressor protein p53, mutations of which appear in approximately half of all human cancers. With a combination of structural and computational data from our collaborators, we have designed a first-generation structure that is predicted to bind to a number of inactive p53 mutants, thereby stabilizing the native structure and restoring function. Combinatorial library synthesis is underway, as are additional ligand design studies.
The overall goal of one project is to understand at a molecular level the interactions between the membrane receptors that mediate excitatory neurotransmission and the endogenous ligand that activates them, glutamic acid. The traditional division of ionotropic glutamate receptors (iGluRs) into three classes (NMDA, AMPA, KA) with distinct pharmacological properties is rapidly becoming obsolete with the recent characterization of multiple sub-types of each class, each likely controlling different functions. Our current goal is to develop sub-type selective ligands that will clearly delineate the distinct functions of each iGluR sub-type. Employing ligand design in conjunction combinatorial library synthesis (often based on structures of natural toxins that interact with iGluR receptors), with these studies may not only lead to a better understanding of such important processes as learning and memory, but also provide new details on mechanisms of brain damage in disorders such as stroke, epilepsy, and Alzheimer's disease.
A second area of interest is the design and synthesis of small molecules that modulate the activity of the important serine-threonine protein phosphatases PP1 and PP2A. Inhibitors such as the naturally occurring toxins okadaic acid, microcystin, and tautomycin have been the only available small molecule probes used by cell biologists to study the respective roles of PP1 and PP2A in cellular signaling pathways. Using these natural products as "lead" compounds, we are designing and synthesizing simplified analogues with improved selectivity or other valuable properties. For example, we have recently shown that highly truncated versions of microcystin and tautomycin retain nanomolar activities (albeit at significantly reduced levels compared to the parent toxins) and thus provide relatively easy-to-prepare scaffolds for exciting new studies of in vivo imaging of phosphatase trafficking via fluorescently labeled versions of the truncated compounds.
Applying a similar general strategy, we are designing new compounds based on the structure of the natural terpenoid correolide, which has recently been reported to be a potent blocker of certain types of potassium channels that are particularly abundant in the T-cells of the immune system. The goal is to discover a more selective blocker, preferably with a considerably simpler structure, that would serve as a lead compound for a new type of immunosuppressant drug.
Finally, we are working on several collaborative projects with fellow UCI Comprehensive Cancer Center members to develop new types of anti-tumor compounds. Many labs have made substantial progress in the past several years in developing effective chemotherapeutic agents for the treatment of HIV infection, but there remains a substantial demand for new strategies. Our approach is to employ computational ligand-based design in conjunction with combinatorial library synthesis to develop new HIV Integrase (IN) inhibitors based on the natural product IN inhibitor chicoric acid. We are also participants in a separate exciting collaboration that targets the tumor suppressor protein p53, mutations of which appear in approximately half of all human cancers. With a combination of structural and computational data from our collaborators, we have designed a first-generation structure that is predicted to bind to a number of inactive p53 mutants, thereby stabilizing the native structure and restoring function. Combinatorial library synthesis is underway, as are additional ligand design studies.
Publications
Glauber KM, Dana CE, Park SS, Colby, DA, Noro Y, Fujisawa T, Chamberlin AR, and Steele RE. Develop., 2013, in press. “A Small Molecule Screen Identifies a Novel Compound that Induces a Homeotic Transformation in Hydra.”
Zhu J, Zhou L, Wu G, Konig H, Lin X, Li G, Qiu X-L, Chen C-F, Goldblatt E, Bhatia R, Chamberlin AR, Chen, P-L, and Lee W-H. EMBO Mol. Med., 2013, Jan 22. doi: 10.1002/emmm.201201760. [Epub ahead of print].
Wassman CD, Baronio R, Demir Ö, Wallentine BD, Chen C-K, Hall LV, Salehi F, Da-Wei Lin D-W, Chung BP, Hatfield GW, Chamberlin AR, Luecke H, Lathrop RH, Kaiser P and Amaro RE. Nature Commun., 2013, 4, 1407 “Computational Identification of a Transiently Open L1/S3 Pocket for p53 Cancer Mutant Reactivation.”
Delisle Milton RC, Milton SC, Chamberlin AR. Int J Pept Res Ther. 2012, 17, 337-342. “Improving the Fmoc Solid Phase Synthesis of the Cyclic Hexapeptide Complement C5a Antagonist PMX205.” PMID: 22707924
Carroll, CL and Chamberlin, AR Tetrahedron Lett. 2011, 52, 3995-3997. “Synthesis of the dysiherbaine tetrahydropyran core utilizing improved tethered aminohydroxylation conditions.”
Demir Ö, Baronio R, Salehi F, Wassman CD, Hall L, Hatfield GW, Chamberlin AR, Kaiser P, Lathrop RH, and Amaro RE PLoS Comp. Bio, 2011,e1002238. doi:10.1371/journal.pcbi.1002238 “Ensemble-based Computational Approach Discriminates p53 Functional Activity.” PMC3197647
Mihailescu, M; Vaswani, RG; Jardon-Valadez, E; Castro-Roman, F; Freites, JA; Worcester, DL; Chamberlin, AR; Tobias, DJ; White, SH. Biophysical Journal 2011,100, 1455-1462. “Acyl-Chain Methyl Distributions of Liquid-Ordered and -Disordered Membranes.”
Ziolkowski LA, Chamberlin AR, J. Greaves J, Druffel ERM. Limnol. Oceanogr. Methods 2011, 9, 140. ”Quantification of black carbon in marine systems using the benzene polycarboxylic acid method: a mechanistic and yield study.” DOI: 10.4319/lom.2011.9.140
Glauber, K.M.; Dana, C.E.; Park, S.S.; Li, T.; Chamberlin, R.A.; Steele, R.E. Dev Biol 2010, 344, 451. “Dissecting Tentacle Formation in Hydra Using Chemical Genetics.” DOI: 10.1016/j.ydbio.2010.05.158. PMID 20933774
Limon, A.; Reyes-Ruiz, J.M.; Vaswani, R.G. ; Chamberlin, A. R.; Miledi, R. ACS Chem. Neurosci. 2010 1, 175–181. “Kaitocephalin Antagonism of Glutamate Receptors Expressed in Xenopus Oocytes.” DOI: 10.1021/cn900037c
Qiu XL, Li G, Wu G, Zhu J, Zhou L, Chen PL, Chamberlin AR, Lee WH. J Med Chem. 2009 52,1757-1767 “Synthesis and Biological Evaluation of a Series of Novel Inhibitor of Nek2/Hec1 Analogues.” PMID: 19243176
Qiu, X.; Zhu, J.; Wu, G.; Lee, W.-H. ; Chamberlin, A.R. J. Org. Chem 2009, 74, 2018–2027. "Stereoselective Synthesis of Chiral IBR2 Analogues."
Habay, S.A.; Park, S.S.; Kennedy, S.M.; Chamberlin, A.R., Chapter in Amino Acids, Peptides and Proteins in Organic Chemistry, Vol. I (A. Hughes, ed.), Wiley-VCH, 2009, pp. 163-244. . “Methods for the Chemical Synthesis of Non-Coded alpha-Amino Acids found in Natural Product Peptides.”
Vaswani, R.G.; Limon, A.; Reyes-Ruiz, J.M.; Miledi, R; Chamberlin, A. R. Bioorg. Med. Chem. Lett. 2009, 19, 132-135. “Design, Synthesis, and Biological Evaluation of a Scaffold for iGluR Ligands Based on the Structure of (–)-Kaitocephalin.”
Wu, G.; Qiu, X.; Zhou, L.; Zhu, J.; Chamberlin, A.R.; Lau, J. P.-L.; Chen, P.-L.; Lee, W.-H. Cancer Res. 2008, 68, 8393-8399. "Small molecule targeting mitotic regulator Hec1 suppresses tumor cell growth in culture and in animals."
Okamura, N.; Habay, S.H.; Zeng, J. A.; Chamberlin, A.R.; Reinscheid, R.K. J. Pharmacol Exp. Ther. 2008, 325, 893-901.. “Synthesis And Pharmacological In Vitro And In Vivo Profile Of SHA 68 (3-Oxo-1,1-Diphenyl-Tetrahydro-Oxazolo[3,4-A]Pyrazine-7-Carboxylic Acid 4-Fluoro-Benzylamide), A Selective Antagonist Of The Neuropeptide S Receptor.”
Vaswani, R.G.; Chamberlin, A. R. J. Org. Chem. 2008, 73, 1661-1681. “Stereocontrolled Total Synthesis of (–)-Kaitocephalin.”
Tappan, E.M.; Chamberlin, A. R. Chem&Biol, 2008,15, 167-174. “Activation of Protein Phosphatase-1 by a Small Molecule Designed to Bind to the Allosteric Regulatory Site.”
Cohen, J.L.; Chamberlin, A. R. J. Org. Chem. 2007, 74, 9240-9247. “Diastereoselective Synthesis of Glutamate-Appended Oxolane Rings: Synthesis of (S)-(+)-Lycoperdic Acid.”
Cohen, J.L.; Chamberlin, A. R. Tetrahedron Lett. 2007, 48, 2533-2536. “Synthesis of the Dysiherbaine Tetrahydropyran Core Employing a Tethered Aminohydroxylation Reaction.”
Colby, D. A.; Chamberlin, A. R. Mini-reviews in Med. Chem. 2006, 6, 657-665 “Pharmacophore Identification: The Case of the Ser/Thr Protein Phosphatase Inhibitors.”
Cohen, J.L.; Limon, A.; Miledi, R; Chamberlin, A. R. J. Org. Chem. 2006, 16, 2189-2194. “Design, Synthesis, and Biological Evaluation of a Scaffold for iGluR Ligands Based on the Structure of (–)-Dysiherbaine.”
Charvat, T.T.; Lee, D.; Robinson, W.E.; Chamberlin, A.R. Bioorg. Med. Chem. 2006, 14, 4552-4567. “Design, Synthesis, and Biological Evaluation of Chicoric Acid Analogs as Inhibitors of HIV-1 Integrase.”
Esslinger, C.S.; Agarwal, S.; Gerdes, J.; Wilson, P.A.; Davis, E.S.; Awes, A.N.; O'Brien, E.; Mavencamp, T.; Koch, H.P.; Poulsen, D.J.; Rhoderick, J.F.; Chamberlin, A.R.; Kavanaugh, M.P.; Bridges, R.J. Neuropharmacology 2005, 49, 850-861. “The gamma-Substituted Aspartate Analogue L-?-threo-Benzyl-Aspartate Preferentially Inhibits the Neuronal Excitatory Amino Acid Transporter EAAT3”
Sandler, J.S.; Fenical, W.; Gulledge, B.M.; Chamberlin, A.R.; La Clair, J.J. J. Am. Chem. Soc. 2005, 127, 9320-9321. “Fluorescent Profiling of Natural Product Producers.”
Hart, M.E.; Chamberlin, A. R.; Walkom, C.; Sakoff, J.A.; McCluskey, A. Bioorg. Med. Chem. Lett. 2004, 14, 1969-1973. “Modified Norcantharidins: Synthesis, Protein Phosphatases 1 and 2A Inhibition, and Anticancer Activity.”
Shou, X.; Chamberlin, A. R. Exp. Opin. Ther. Patents 2004,14, 471-486. “Ligands for Kainate Subtype Glutamate Receptors.”
Gulledge, B.M.; Aggen, J.B.; Chamberlin, A.R. Bioorg. Med. Chem. Lett. 2003, 13, 2903-2906. “Linearized and Truncated Microcystin Analogues as Inhibitors of Protein Phosphatases 1 and 2A.”
Gulledge, B.M.; Aggen, J.B.; Eng, H.; Sweimeh, K.; Chamberlin, A.R. Bioorg. Med. Chem. Lett. 2003, 13, 2907-2911. “Microcystin Analogues Comprised Only of Adda and a Single Additional Amino Acid Retain Moderate Activity as PP1/PP2A Inhibitors.”
Colby, D.A.; Liu, W; Sheppeck, J.E, Jr.; Huang, H.-B.; Nairn, A. C.; Chamberlin, A.R. Bioorg. Med. Chem. Lett. 2003, 13, 1601-1605. “A New Model of the Tautomycin-PP1 Complex That Is Not Analogous to the Corresponding Okadaic Acid Structure.”
Liu, W; Sheppeck, J.E, Jr.; Colby, D.A.; Huang, H.-B.; Nairn, A. C.; Chamberlin, A.R. Bioorg. Med. Chem. Lett. 2003, 13, 1597-1600. “The Selective Inhibition of Phosphatases by Natural Toxins: the Anhydride Domain of Tautomycin is Not a Primary Factor in Controlling PP1/PP2A Selectivity.”
Gulledge, B.; Aggen, J.B.; Huang, H-B.: Nairn, A.C.; Chamberlin, A.R. Curr. Med. Chem. 2002, 9. 1991-2003. “The Microcystins and Nodularins: Cyclic Polypeptide Inhibitors of PP1 and PP2A.”
Arai, A.C.;Xia, Y.-F; Kessler, M.; Phillips, D.; Chamberlin, A.R. ; Granger, R.; Lynch, G. Mol. Pharm. 2002, 62, 566-577. “Effects of 5'-alkyl-benzothiadiazides on AMPA receptor biophysics and synaptic responses.”
Krutzik, P.O.; Chamberlin, A.R. In Combinatorial Library Methods and Protocols, Methods in Molecular Biology; English, L.B. Ed.; Humana: Totowa, NJ, 2002; Ch. 6. ”Synthesis of DNA-binding Polyamides: Robust Solid-phase Methods for Coupling Heterocyclic Aromatic Amino Acids.”
Krutzik, P.O.; Chamberlin, A. R. Bioorg. Med. Chem. Lett.. 2002, 12, 2129-2132. “Rapid Solid-phase Synthesis of DNA-binding Pyrrole-imidazole Polyamides.”
Esslinger, C.S.; Titus, J.L.; Koch, H.P.; Bridges, R.J.; Chamberlin, A.R. Bioorg. Med. Chem. Lett. 2002, 10, 3509-3515. “Methylation of L-trans-2,4-Pyrrolidine Dicarboxylate Converts the Glutamate Transport Inhibitor from a Substrate to a Non-substrate Inhibitor.”
Lew, A.; Krutzik, P.O.; Hart, M. E.; Chamberlin, A. R. J. Comb. Chem. 2002, 4, 95-105. “Increasing Rates of Reaction: Microwave-assisted Organic Synthesis for Combinatorial Chemistry.”
Lew, A.; Chamberlin, A. R. In Combinatorial Library Methods and Protocols, Methods in Molecular Biology; English, L.B. Ed.; Humana: Totowa, NJ, 2002; Ch. 7. “Preparation of Phenyl-stilbene Derivatives Using the Safety Catch Linker.”
Phillips, D.; Chamberlin, A.R. J. Org. Chem. 2002, 67, 3194-3201. “Total Synthesis of Dysiherbaine.”
Vaswani, R.G.; Chamberlin, A. R. J. Org. Chem. 2008, 73, 1661-1681. “Stereocontrolled Total Synthesis of (–)-Kaitocephalin.”
Tappan, E.M.; Chamberlin, A. R. Chem&Biol, 2008,15, 167-174. “Activation of Protein Phosphatase-1 by a Small Molecule Designed to Bind to the Allosteric Regulatory Site.”
Cohen, J.L.; Chamberlin, A. R. J. Org. Chem. 2007, 74, 9240-9247. “Diastereoselective Synthesis of Glutamate-Appended Oxolane Rings: Synthesis of (S)-(+)-Lycoperdic Acid.”
Cohen, J.L.; Chamberlin, A. R. Tetrahedron Lett. 2007, 48, 2533-2536. “Synthesis of the Dysiherbaine Tetrahydropyran Core Employing a Tethered Aminohydroxylation Reaction.”
Colby, D. A.; Chamberlin, A. R. Mini-reviews in Med. Chem. 2006, 6, 657-665 “Pharmacophore Identification: The Case of the Ser/Thr Protein Phosphatase Inhibitors.”
Cohen, J.L.; Limon, A.; Miledi, R; Chamberlin, A. R. J. Org. Chem. 2006, 16, 2189-2194. “Design, Synthesis, and Biological Evaluation of a Scaffold for iGluR Ligands Based on the Structure of (–)-Dysiherbaine.”
Charvat, T.T.; Lee, D.; Robinson, W.E.; Chamberlin, A.R. Bioorg. Med. Chem. 2006, 14, 4552-4567. “Design, Synthesis, and Biological Evaluation of Chicoric Acid Analogs as Inhibitors of HIV-1 Integrase.”
Esslinger, C.S.; Agarwal, S.; Gerdes, J.; Wilson, P.A.; Davis, E.S.; Awes, A.N.; O'Brien, E.; Mavencamp, T.; Koch, H.P.; Poulsen, D.J.; Rhoderick, J.F.; Chamberlin, A.R.; Kavanaugh, M.P.; Bridges, R.J. Neuropharmacology 2005, 49, 850-861. “The gamma-Substituted Aspartate Analogue L-?-threo-Benzyl-Aspartate Preferentially Inhibits the Neuronal Excitatory Amino Acid Transporter EAAT3”
Sandler, J.S.; Fenical, W.; Gulledge, B.M.; Chamberlin, A.R.; La Clair, J.J. J. Am. Chem. Soc. 2005, 127, 9320-9321. “Fluorescent Profiling of Natural Product Producers.”
Hart, M.E.; Chamberlin, A. R.; Walkom, C.; Sakoff, J.A.; McCluskey, A. Bioorg. Med. Chem. Lett. 2004, 14, 1969-1973. “Modified Norcantharidins: Synthesis, Protein Phosphatases 1 and 2A Inhibition, and Anticancer Activity.”
Shou, X.; Chamberlin, A. R. Exp. Opin. Ther. Patents 2004,14, 471-486. “Ligands for Kainate Subtype Glutamate Receptors.”
Gulledge, B.M.; Aggen, J.B.; Chamberlin, A.R. Bioorg. Med. Chem. Lett. 2003, 13, 2903-2906. “Linearized and Truncated Microcystin Analogues as Inhibitors of Protein Phosphatases 1 and 2A.”
Gulledge, B.M.; Aggen, J.B.; Eng, H.; Sweimeh, K.; Chamberlin, A.R. Bioorg. Med. Chem. Lett. 2003, 13, 2907-2911. “Microcystin Analogues Comprised Only of Adda and a Single Additional Amino Acid Retain Moderate Activity as PP1/PP2A Inhibitors.”
Colby, D.A.; Liu, W; Sheppeck, J.E, Jr.; Huang, H.-B.; Nairn, A. C.; Chamberlin, A.R. Bioorg. Med. Chem. Lett. 2003, 13, 1601-1605. “A New Model of the Tautomycin-PP1 Complex That Is Not Analogous to the Corresponding Okadaic Acid Structure.”
Liu, W; Sheppeck, J.E, Jr.; Colby, D.A.; Huang, H.-B.; Nairn, A. C.; Chamberlin, A.R. Bioorg. Med. Chem. Lett. 2003, 13, 1597-1600. “The Selective Inhibition of Phosphatases by Natural Toxins: the Anhydride Domain of Tautomycin is Not a Primary Factor in Controlling PP1/PP2A Selectivity.”
Gulledge, B.; Aggen, J.B.; Huang, H-B.: Nairn, A.C.; Chamberlin, A.R. Curr. Med. Chem. 2002, 9. 1991-2003. “The Microcystins and Nodularins: Cyclic Polypeptide Inhibitors of PP1 and PP2A.”
Arai, A.C.;Xia, Y.-F; Kessler, M.; Phillips, D.; Chamberlin, A.R. ; Granger, R.; Lynch, G. Mol. Pharm. 2002, 62, 566-577. “Effects of 5'-alkyl-benzothiadiazides on AMPA receptor biophysics and synaptic responses.”
Krutzik, P.O.; Chamberlin, A.R. In Combinatorial Library Methods and Protocols, Methods in Molecular Biology; English, L.B. Ed.; Humana: Totowa, NJ, 2002; Ch. 6. ”Synthesis of DNA-binding Polyamides: Robust Solid-phase Methods for Coupling Heterocyclic Aromatic Amino Acids.”
Krutzik, P.O.; Chamberlin, A. R. Bioorg. Med. Chem. Lett.. 2002, 12, 2129-2132. “Rapid Solid-phase Synthesis of DNA-binding Pyrrole-imidazole Polyamides.”
Esslinger, C.S.; Titus, J.L.; Koch, H.P.; Bridges, R.J.; Chamberlin, A.R. Bioorg. Med. Chem. Lett. 2002, 10, 3509-3515. “Methylation of L-trans-2,4-Pyrrolidine Dicarboxylate Converts the Glutamate Transport Inhibitor from a Substrate to a Non-substrate Inhibitor.”
Lew, A.; Krutzik, P.O.; Hart, M. E.; Chamberlin, A. R. J. Comb. Chem. 2002, 4, 95-105. “Increasing Rates of Reaction: Microwave-assisted Organic Synthesis for Combinatorial Chemistry.”
Lew, A.; Chamberlin, A. R. In Combinatorial Library Methods and Protocols, Methods in Molecular Biology; English, L.B. Ed.; Humana: Totowa, NJ, 2002; Ch. 7. “Preparation of Phenyl-stilbene Derivatives Using the Safety Catch Linker.”
Phillips, D.; Chamberlin, A.R. J. Org. Chem. 2002, 67, 3194-3201. “Total Synthesis of Dysiherbaine.”
Grants
National Institutes of Health (R01 NS27600) $920.000
P.I., 2004-2009
“Receptor-Specific Excitatory Amino Acid Analogues”
National Institutes of Health (R01 GM57550) $760,000
P.I., 2004-2009
“New Signaling Pathway Probes Based on Natural Toxins”
National Institutes of Health (1P01GM086685)
$850,000
Program Project Core Director, 2009-14
"Making Sense of Voltage Sensors"
National Institutes of Health/NCI (T32 CA113265)
$310,999,
Training Faculty,
2007-12
“Translational Research in Cancer Genomic Medicine”
MRPI 143226, University of California, (W. E. Robinson, PI) 2/1/10-6/30/15 ADC $50K
California Center for Antiviral Drug Discovery
This grant funds a multi-campus research consortium focused on developing anti-viral drugs. The Chamberlin group is synthesizing libraries of HIV integrase inhibitors in collaboration with the PI.
Role: Collaborator
NIH, P01 GM086685-01 (S. White, PI) 2/1/09-1/31/14 ADC $140,000
Making Sense of Voltage Sensors
The major goal of this project is to probe the structure and dynamics of voltage-gated potassium ion channels. Chamberlin provides the specifically deuterated lipids, amino acids and proteins that are essential to the completion of two of the individual projects.
Role: Core Director
NIH, 5R01NS035144 (A. Tenner, PI) 04/01/2010 – 03/30/2015 ADC $10K
C5a Receptor Antagonist as a Therapy to Slow the Progression of Alzheimer’s Disease
The Chamberlin group’s role in this project is to optimize the properties of a family of cyclic peptide antagonists of the C5a receptor.
Professional Societies
American Chemical Society
American Association for the Advancement of Science
Society for Neuroscience
Graduate Programs
Chemical Biology
Medicinal Chemistry and Pharmacology
Research Centers
UCI Comprehensive Cancer Center
UCI Institute for Brain Aging and Dementia
Link to this profile
https://faculty.uci.edu/profile/?facultyId=4902
https://faculty.uci.edu/profile/?facultyId=4902
Last updated
09/30/2013
09/30/2013