Andisheh Abedini, PhD, Postdoctoral Fellow

Dr. Abedini is interested in the role of RAGE in diabetes and metabolic disorders. Her current research focuses on the molecular and cellular mechanisms of RAGE in human amyloidosis and type 2 diabetes; with an emphasis on the development of rationally designed inhibitors of RAGE-mediated toxicity.

Dr. Abedini received her PhD from the State University of New York at Stony Brook where she trained in biophysics and peptide chemistry. She joined Professor Ann Marie Schmidt’s research team in 2009 after training at the Joslin Diabetes Center at Harvard Medical School and spending one year as a Visiting Fellow at the Child and Family Research Institute at the University of British Columbia.

 

Peer-Reviewed Publications
1. Wang H, Abedini A, Ruzsicska BP, Raleigh DP. Rationally Designed, Non-Toxic, Non-Amyloidogenic Analogs of Human Islet Amyloid Polypeptide with Improved Solubility. (2014) Biochemistry 53(37):5876-84.

2. Cao P, Abedini A, Wang H, Tu LH, Zhang X, Schmidt AM, Raleigh DP. Islet amyloid polypeptide toxicity and membrane interactions. (2013) Proc Natl Acad Sci USA 110(48):19279-84.

3. Abedini A, Schmidt AM. Mechanisms of islet amyloidosis toxicity in type 2 diabetes. (2013) FEBS Lett. 587(8):1119-27.

4. Cao P, Abedini A, Raleigh DP. Aggregation of islet amyloid polypeptide: from physical chemistry to cell biology. (2013) Curr Opin Struct Biol. 23(1):82-9.

5. Cao P, Marek P, Noor H, Patsalo V, Tu LH, Wang H, Abedini A, Raleigh DP. Islet amyloid: From fundamental biophysics to mechanisms of cytotoxicity. (2013) FEBS Lett. 587(8):1106-18.

6. Ladiwala AR, Bhattacharya M, Perchiacca JM, Cao P, Raleigh DP, Abedini A, Schmidt AM, Varkey J, Langen R, Tessier PM. Rational design of potent domain antibody inhibitors of amyloid fibril assembly. (2012) Proc. Natl. Acad. Sci. USA 109(49):19965-70

7. Cao P, Tu LH, Abedini A, Levsh O, Akter R, Patsalo V, Schmidt AM, Raleigh DP. Sensitivity of amyloid formation by human islet amyloid polypeptide to mutations at residue 20. (2012) J Mol. Biol. 421(2-3):282-95.

8. Meng F, Abedini A, Plesner A, Verchere BC, Raleigh DP. The flavanol (-)-epigallocatechin 3-gallate inhibits amyloid formation by islet amyloid polypeptide, disaggregates amyloid fibrils, and protects cultured cells against IAPP-induced toxicity. (2010) Biochemistry 49(37):8127-33.

9. Meng F, Raleigh DP, Abedini A. Combination of kinetically selected inhibitors in trans leads to highly effective inhibition of amyloid formation. (2010) J. Am. Chem. Soc. 132(41):14340-2.

10. Meng F, Abedini A, Plesner A, Middleton CT, Potter KJ, Zanni MT, Verchere BC, Raleigh, DP. The sulfated triphenyl methane derivative acid fuchsin is a potent inhibitor of amyloid formation by human islet amyloid polypeptide and protects against the toxic effects of amyloid formation. (2010) J. Mol. Biol. 400(3):555-566.

11. Potter K*, Abedini A*, Merek P, Driscoll M, Verchere BC, Raleigh DP. Islet amyloid deposition limits the viability of human islet grafts but not porcine islet cell grafts. (2010) Proc. Natl. Acad. Sci. USA 107(9), 4305-4310. *Joint first authors

12. Cao P, Meng F, Abedini A, Raleigh DP. The ability of rodent islet amyloid polypeptide to inhibit amyloid formation by human islet amyloid polypeptide has important implications for the mechanism of amyloid formation and the design of inhibitors. (2010) Biochemistry 49(5):872-81.

13. Abedini A and Raleigh DP. A critical assessment of the role of helical intermediates in amyloid fibril formation. (2009) Protein Engineering, Design and Selection 22(8):453-459.

14. Abedini A and Raleigh DP. A role for helical intermediates in amyloid formation by natively unfolded polypeptides. (2009) Physical Biology 6(1) article ID 015005.

15. Potter K, Abedini A, Butterworth S, Driscoll M, Marek P, Korbutt G, Fraser P, Verchere C B, Raleigh DP. Lack of amyloidogenicity of pig islet amyloid polypeptide may contribute to improved function and survival of pig islet xenografts. (2008) J. Investigative Med. 56, 134-135.

16. Abedini A and Raleigh DP. Protein Misfolding: Amyloid Formation. (2008) Wiley Encyclopedia of Chemical Biology. John Wiley and Sons.

17. Abedini A, Meng F, Raleigh DP. A single point mutation converts highly amyloidogenic human islet amyloid polypeptide into a potent inhibitor of fibrillization. (2007) J. Am. Chem. Soc. 129(37) 11300-11301.

18. Meng F, Abedini A, Song B, Raleigh DP. Amyloid formation by proIAPP processing intermediates: Examination of the role of protein-heparan sulfate interactions and implications for islet amyloid formation in type 2 diabetes. (2007) Biochemistry 46(43)12091-12099.

19. Marek P, Abedini A, Song B, Kanungo M, Johnson ME, Gupta R, Zaman W, Wong SS, Raleigh DP. Aromatic interactions are not required for amyloid formation by islet amyloid polypeptide but do influence the rate of fibril formation and fibril morphology. (2007) Biochemistry 46(11) 3255-3261.

20. Abedini A*, Tracz SM*, Cho JH, Raleigh DP. Characterization of the heparin binding site in the N-terminus of human pro-islet amyloid polypeptide: Implications for amyloid formation. (2006) Biochemistry 45(30), 9228-9237. *Joint first authors

21. Abedini A, Singh G, Raleigh DP. Recovery and purification of highly aggregation-prone disulfide-containing peptides: Application to islet amyloid polypeptide. (2006) Anal. Biochem. 351, 181-186.

22. Abedini A and Raleigh DP. Destabilization of human IAPP amyloid fibrils by proline mutations outside of the putative amyloidogenic domain: Is there a critical amyloidogenic domain in human IAPP? (2006) J. Mol. Bio. 355(2), 274-281.

23. Abedini A and Raleigh DP. The role of His-18 in amyloid formation by human islet amyloid polypeptide. (2005) Biochemistry 44(49), 16284-16291.

24. Abedini A and Raleigh DP. Incorporation of pseudoproline derivatives allows the facile synthesis of human IAPP; a highly amyloidogenic and aggregation-prone polypeptide. (2005) Organic Letters 7, 693-696.

25. Tracz SM*, Abedini A*, Driscoll M, Raleigh DP. The role of aromatic interactions in amyloid formation by polypeptides: Analysis of peptides derived from human amylin. (2004) Biochemistry 43, 15901-15908. *Joint first authors

Invited Book Chapters and Commentaries

1. Abedini A, Cao P and Raleigh DP. Detection of helical intermediates during amyloid formation by intrinsically disordered polypeptides and proteins. (2014) Methods Mol. Biol. (In Press)

2. Abedini A and Raleigh DP. Islet Amyloid Polypeptide. (2009) In: Protein Misfolding Diseases: Current and Emerging Principles and Therapies. Edited by Dobson, C. M., Kelly, J. W. and Ramirez-Alvarado, M. Published by John Wiley and Sons.

3. Abedini A, Gupta R, Marek P, Meng F, Tracz S, Taskent H and Raleigh DP. Post Translational Modifications and Amyloid Formation. (2009) In: Protein Misfolding Diseases: Current and Emerging Principles and Therapies. Edited by Dobson, C. M., Kelly, J. W. and Ramirez-Alvarado, M. Published by John Wiley and Sons.

4. Abedini A and Shoelson SE. STAMPing out insulin resistance? (2007) Immunology and Cell Biology 85(6): 399-400.

Patents

1. United States Provisional Patent No. 61/520,396 (2011) "Assays and Methods Pertaining to Pre-Amyloid Intermediates". Schmidt AM, Abedini A, Raleigh DP.

2. United States Provisional Patent No. 12/405,519 (2008) "Fluorescent Analogs of the Islet Amyloid Polypeptide". Raleigh DP, Marek P, Meng F, Abedini A and Gupta R.

Invited Talks and Conference Presentations

1. “Is there a common structural basis for amyloid toxicity? A new receptor-mediated mechanism of pancreatic islet amyloid-induced beta-cell toxicity in type 2 diabetes”, (2014) The 28th Symposium of the Protein Society, San Diego, CA, USA.

2. Invited Speaker: “RAGE mediates pancreatic islet amyloidosis-induced beta cell toxicity by binding pre-amyloid amylin intermediates: Implications for type 2 diabetes” (2014) New York Lipid and Vascular Club, The Rockefeller University, New York, NY, USA.

3. Invited Speaker: “Islet amyloidosis induces beta-cell death via pre-fibrillar amylin lag phase intermediates that bind RAGE”, (2013) FASEB: Basic Origins and Medical Consequences of Protein Aggregation, Big Sky, MT, USA.

4. “The chemical biology of RAGE/IAPP interactions involved in the pathogenesis of pancreatic beta cells in type 2 diabetes”, (2013) The New York Academy of Sciences Chemical Biology Discussion Group Year-End Symposium, 7 World Trade Center, New York, NY, USA.

5. Invited Speaker: “Identification and characterization of the toxic species in islet amyloidosis and a new receptor-mediated mechanism of cytotoxicity in type 2 diabetes”, (2013) Lehman College, CUNY, New York, New York, USA.

6. “Structural biology of islet amyloidosis in type 2 diabetes: Interaction of toxic species with the receptor for advanced glycation endproducts (RAGE)”, (2013) The New York Structural Biology Discussion Group 8th Winter Meeting of the New York Academy Of Sciences, 7 World Trade Center, New York, NY, USA.

7. Invited Speaker: “Applying mass spectroscopy to solving biomedical problems in diabetes”, (2012) Biochemistry, Structural Biology and Chemistry Section, The Rockefeller University, New York, NY, USA.

8. “RAGE is a receptor for toxic intermediates produced during IAPP amyloid formation: A molecular basis for islet amyloid induced cell death in type 2 diabetes”, (2012) The New York Academy of Sciences Chemical Biology Discussion Group Year-End Symposium, 7 World Trade Center, New York, NY, USA.

9. Invited Speaker: “The molecular basis of islet amyloid induced cell death”, (2012) The 26th Symposium of the Protein Society, San Diego, CA, USA.

10. Invited Speaker: “RAGE and islet amyloidosis: A mechanism of cellular toxicity in T2D”, (2011) FASEB: Basic Origins and Medical Consequences of Protein Aggregation, Snowmass, CO, USA.

11. Invited Speaker: “Toxic intermediates during IAPP amyloid formation”, (2011) The New York Structural Biology Discussion Group 6th Winter Meeting of the New York Academy Of Sciences, 7 World Trade Center, New York, NY, USA.

12. Invited Speaker: “Mechanism of amyloid formation by IAPP and design of inhibitors of its toxicity and fibrillization”, (2009) Department of Pathology, Child and Family Research Institute, University of British Columbia, Vancouver, B.C, Canada.

13. Invited Speaker: “From insulin resistance to type 2 diabetes: A biological and biophysical perspective”, (2008) Department of Surgery, Division of Surgical Sciences, Columbia University Medical Center, New York, NY, USA.

14. Invited Speaker: “From insulin resistance to type 2 diabetes: A biological and biophysical perspective”, (2008) Biochemistry, Structural Biology and Chemistry Section, The Rockefeller University, New York, NY, USA.

15. Invited Speaker: “Adipose tissue macrophages and pathological inflammation in obesity-induced insulin resistance”, (2008) Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany.

16. Invited Speaker: “Mechanistic and structural insight into amyloid formation by islet amyloid polypeptide: Implications for type 2 diabetes”, (2006) Diabetes and Metabolism Research Unit, Boston Medical Center, Boston, MA, USA.

17. “Amyloid formation by human islet amyloid polypeptide”, (2006) The Keystone Symposium on Protein Misfolding Diseases: Mechanisms of Misfolding, Pathology and Therapeutic Strategies, Breckenridge, CO, USA.

18. “The role of His-18 in amyloid assembly and morphology of human islet amyloid polypeptide”, (2005) The 19th Symposium of the Protein Society, Boston, MA, USA.

19. “The role of His-18 in amyloid assembly and morphology of human islet amyloid polypeptide”, (2005) The US-Japan Symposium on Protein Folding, Design and Dynamics, Philadelphia, PA, USA.

20. “Insight into the amyloidogenicity of human islet amyloid polypeptide”, (2004) Protein Misfolding, Amyloid and Conformational Disease, Snowmass, CO, USA.

21. “Insight into the amyloidogenicity of human islet amyloid polypeptide”, (2004) The 18th Symposium of the Protein Society, San Diego, CA, USA.

22. Invited Speaker: “Carnegie Initiative on the Doctorate (CID) assessment of doctoral programs: Northeastern, Stony Brook, Colorado and Ohio State”, (2004) The 228th National Meeting of the American Chemical Society, Philadelphia, PA, USA.

23. “Formation and decomposition of 2-(2-phenylethyl)-imidazoline”, (2001) 221st American Chemical Society, San Diego, CA, USA.