Principal Scientist

SHANKARAMMA SHIVAPRASAD

***** ******** **** ********** ** 20871

Home: 717-***-**** Cell: 301-***-****

Visa status: U.S. Citizen Email: ***********@*****.***

Summary

Versatile biotechnology professional with broad expertise in experimental design, development and execution of analytical and biochemical assays as well as project management.

Experience and Strengths

• 12 years experience in peptide/protein characterization and Drug discovery research, biochemical assay development.

• Experience in in-vitro diagnostic assay development to detect mis-folded proteins in clinical samples.

• Extensive knowledge in peptide design for target protein binding, structural biology, protein purification and characterization using various analytical techniques.

• Trouble shooting

• Effective at supervising scientific staff, establishing and supporting collaborations with Biopharm/academic labs.

• Published research accomplishments in peer-reviewed publications, review articles, book chapters, patents and presentations at conferences. Good communication and presentation skills.

Employment History

2008-present Principal Scientist, Lancaster Laboratories, Lancaster, PA

Field: Characterization of biomolecules such as monoclonal antibody, vaccines and other protein therapeutics using high resolution tandem mass spectrometers under cGMP guidelines.

Achievements:

• Developed and validated methods for characterization, identification and quantitation of biomolecules (peptide mapping, post-translational modifications, glycoprofilling and N-terminal sequencing) using mass spectrometer.

• Supervised and trained scientific staff to meet project goal.

• Initiated and managed various training courses on application of different mass spectrometry instruments for the team members.

• Entrusted with complex client technical issues as a result of exceptional knowledge and ability to resolve concerns and satisfy clients.

• Thorough knowledge of FDA Guidance for the Industry, and ICH Guidelines as they relate to drug substance and drug product characterization, control, and stability.

• Represented the company and presented work in professional meetings.

2006-2008 Scientist - Senior Scientist, Adlyfe Inc. Rockville MD

Field: Protein folding platform technology and its application to mis-folded protein disease detection particularly for Alzheimer’s disease diagnosis.

Achievements:

• As a lead scientist, contributed significantly towards the biochemical assay development for early detection of Alzheimer’s disease.

• Promoted from research scientist to senior scientist within six months of joining the company.

• Designed and developed matrix analysis to evaluate various parameters during assay development – pH, solvent/buffer , metal ions, temperature, time course and protein concentration.

• Managed in-house and outsourced research activities.

• Initiated and managed company collaborations with academic labs and contract research labs.

• Authored a patent application with broad claims on platform blood barrier technology.

• Created and directed QC activity for characterization of protein and peptide molecules.

• Responsible for providing technical expertise for trouble shooting in QC, research and assay development.

• Presented company technology in professional meetings and to collaborators.

2002-2006 Senior Research Associate, UT Medical Center, Knoxville, TN.

Field: Broad spectrum of understanding the mechanism of neurodegenerative disease related to Alzheimer’s disease.

Achievements:

• Achieved research goals of developing a technique to understand the aggregation mechanism and structure of amyloid fibrils and oligomers.

• Executed NIH funded projects independently to understand the structural assembly of amyloid beta peptide aggregates by proline, alanine and cysteine scanning mutagenesis studies.

• Established research collaborations with bioinformatics and structural biology groups.

• Supervised and trained interns and other group members in developing new methods for purification, characterization of hydrophobic peptides by HPLC and LC-MS and supervised instrument maintenance and trouble shooting.

• Actively involved in writing grants and manuscripts.

• Published articles in peer reviewed journals, written review article and book chapters.

2000-2002 Postdoctoral Researcher at the University of Zurich, Switzerland

• Design, synthesis, purification and conformational studies of antimicrobial peptides and antimalarial peptides. An industrial collaborated project and work was carried out under GLP environment.

• Design, synthesis and conformational studies on template-constrained beta-hairpin mimetics to understand the protein-protein/protein-ligand interactions.

• Authored 2 patents with claims on the peptidomimetic design for new drug discovery.

• Trained graduate students in executing the project and supervised their work in the lab.

1997-1999 CSIR Research Associate at Indian Institute of Science, Bangalore, India with Prof. P.Balaram, http://mbu.iisc.ernet.in/~pbgrp/pbcv.html

• Design and conformational studies of synthetic peptides to mimic secondary structure of proteins for therapeutic application.

• Structural analysis of de-novo designed peptides using biophysical techniques like NMR and Circular Dichroism (CD).

• Maintenance of lab equipnments like peptide synthesizer, various HPLCs and spectrophotometers.

• Training group members to analyze samples by ESI-MS and MALDI-TOF.

• Supervised and trained summer graduate student in the lab.

1995-1996 Associate scientific manager at Syngene International Pvt. Ltd., Bangalore, India.

• Developed methods for large-scale preparation of N - and side-chain protected amino acids under GMP conditions.

• Supervised a team of six research associates in the development lab.

• Quality control of the samples prepared in the company to meet ISP standards.

• Managing project timelines and preparing project reports and data analysis.

1989-1995 Ph.D. Research Fellow at Bangalore University, Bangalore, India,

Thesis Title: Studies of biologically active peptides and new methodologies for peptide synthesis.

• Design, synthesis and structure-activity studies on analgesic peptides and peptide hormones.

• Developed new methodology for solid phase synthesis of oxytocin using Boc chemistry.

• Prepared O-glycosylated amino acid and used then in the synthesis of analgesic peptides.

• Structure-activity studies on the penta-peptide fragment of Laminin known to inhibit lung tumor colonies in mice.

• Established collaboration to study the activity of designed peptides by using various bio-assays.

Skills

• Analytical techniques:

• Chromatography (SEC, UPLC, HPLC) for protein and peptide purification. Experience in method development, validation and their maintenance.

• Mass spectrometer (MALDI-TOF, ESI-TOF, LC-MS/MS). Familiar with Agilent LC/MSD 1100, LC-ESI-TOF, Voyager MALDI_TOF, Thermo Electron LTQ-orbitrap, Vantage and Water’s micromass LC-MS/MS.

• ELISA techniques with antibody, fluorescence based assay development.

• Gel electrophoresis, dot blot and western blot analysis.

• Amino acid analyzer and peptide sequencer.

• Spectroscopy

• NMR (1D, 2D (DQF-COSY, TOCSY and NOESY)), UV-visible, Circular Dichroism, Fluorescence.

• Biological assay

• Hemolytic assay (human RBCs), E.coli, Staphylococcus and Pseudomonas assay for screening wide array of anti-microbial peptides.

• ELISA/microtiter plate assay technique to determine the binding affinity of antibodies and other immunoassays.

• Selective capture assay using magnetic beads for sample preparation with clinical sample.

• Fluorescence assay to detect misfolded proteins in clinical samples (blood, plasma and CSF).

Patent

• PCT Int. Appl.(2004), 139 pp. CODEN: PIXXD2 WO2004033489 A1 20040422. Template-fixed peptidomimetics with antimicrobial activity. Vrijbloed, Jan Wim; Obrecht, Daniel; Locurio, Sergio; Gombert, Frank; Ludin, Christian; Robinson, John Anthony; Lederer, Alexander; Shankaramma, Shivaprasad. (Polyphor Ltd., Switz.; Universitaet Zuerich).

Book Chapter

• Analysis of amyloid fibril structure by scanning cysteine mutagenesis. Shankaramma Shivaprasad and Ronald Wetzel, Methods in Enzymology, Amyloid II, 2005 edition.

List of publications

I have published 20 peer reviewed articles and some of them are listed below:

1. Wetzel R.; Shankaramma S.; Williams A. Plasticity of amyloid fibrils. Biochemistry 2007, 46 (1), 1-10.

2. Shankaramma S.; Wetzel R., Scanning cysteine mutagenesis analysis of A (1-40) amyloid fibrils. J. Biol. Chem. 2006, 281(2), 993-1000.

3. Brian O’Nuallain; Shankaramma S.; Indu K.; Wetzel R. Thermodynamics of A (1-40) amyloid fibril elongation. Biochemistry 2005, 44(38), 127**-*****.

4. Robinson, John A.; Shankaramma, S. C.; Jetter, Peter; Kienzl, Ursula; Schwendener, Reto A.; Vrijbloed, Jan W.; Obrecht, Daniel., Properties and structure-activity studies of cyclic -hairpin peptidomimetics based on the cationic antimicrobial peptide protegrin I. Bioorganic & Medicinal Chemistry 2005, 13(6), 2055-2064.

5. Shankaramma S.; Wetzel. R., An intersheet packing interaction in A fibrils mapped by disulfide cross-linking. Biochemistry 2004, 43, 153**-*****.

6. Shankaramma, S.C.; Moehle, K.; James, S.; Vrijbloed, J.W.; Obrecht, D.; Robinson, J.A., A family of macrocyclic antibiotics with a mixed peptide-peptoid ß-hairpin backbone conformation. Chem. Comm., 2003, 1842-1843.

7. Shankaramma, S.C.; Athanassiou, Z.; Zerbe, O.; Moehle, K.; Mouton, C.; Bernardini, F.; Vrijbloed, J.W.; Obrecht, D.; Robinson, J.A., Macrocyclic hairpin mimetics of the cationic antimicrobial peptide Protegrin-I: A new family of broad spectrum antibiotics. ChemBiochem. 2002, 3, 1126-1133.

8. Venkataraman, J.; Shankaramma, S.C.; Balaram, P. Design of folded peptides. Chem. Rev. 2001, 101, 3131-3152.

9. Sivanandaiah, K.M.; Suresh Babu, V.V.; Shankaramma, S.C. Solid-phase synthesis of oxytocin using Iodotrichlorosilane as Boc deprotecting agent. Int. J. Peptide Protein Res. 1995, 45, 377-37

10. Sivanandaiah, K.M.; Suresh Babu, V.V.; Shankaramma, S.C. Synthesis of peptides mediated by KOBt. Int. J. Peptide Protein Res. 1994, 44, 24-30.

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