Curriculum Vitae of KATIUSCIA PAGANO
Address: ISMAC-CNR, Via Edoardo Bassini, 15, 20133 Milano
e-mail: katiuscia.pagano@ismac.cnr.it.
Date and Place of Birth: January, 28th 1975 Campi Salentina (LE).
Education:
2008 PhD in Biomedical and Biotechnological Sciences at the Biophysics Research Group, Biomedical
Sciences and Technologies Department, Udine University. Thesis: “NMR structure and functional
characterization of model amyloidogenic proteins”
2003 Board certificate to practice as a professional chemist after a public examination.
2002 Degree in Chemistry, Padova University, Italy. Thesis: “Conformational study of helical peptides in
TFE by Nuclear Magnetic Resonance"
Research Activity
Padova University
Aib-Rich Peptides: Evidence of 310-helix formation
During the degree thesis (2001-2002) Katiuscia Pagano (KP) studied Aib-rich side-chain lactam-bridged
oligomers Ac–(Glu–Aib–Aib–Lys)n–Ala–OH with n =1,2,3 that were designed and synthesized as putative
models of the 310-helix. KP demonstrated by NMR and restrained molecular dynamics simulations that the
three peptides were structured in 310 helix conformation, she thus delineated the characteristic features of a
CD spectrum for a 310-helical structure. Indeed, while the CD spectrum of the α-helical conformation was
very well established, the CD properties of a 310-helix was a much debated problem.
Udine University
Structure and functional characterization of model amyloidogenic proteins
In 2003-2004 KP won a grant from the Biomedical Sciences and Technologies Department, Udine
University. She worked on amyloidosis, a class of pathologies caused by protein misfolding and aggregation.
KP solved the NMR structure of the Hyperthermophilic Sulfolobus solfataricus Acylphosphatase (Sso AcP)
(PDB id 1Y9O), a model fibrillogenic protein. She also performed the structural analysis of the factor
responsible for Sso AcP thermostability with respect to mesophilic AcP's, revealing the importance of a ion
pair network stabilizing secondary structure elements of the protein.
During the PhD period (2005-2007) she developed the following projects:
-study of Sso AcP mechanism of fibril formation under different solution conditions;
-a novel fibril forming acylphosphatase from Eschaerichia Coli: structure determination and aggregation
mechanism investigation;
-development of a new NMR method for the determination of dihedral angles in 15N-labelled peptides and
1
15
protein. Exploiting the resolution of auto- and cross-peaks in 2D H– N HSQC-TOCSY experiments, the
3
3
method estimates JHN-Hα and JHα-Hβ coupling constants from the time evolution of the peaks.
Utrecht University (The Netherlands)
Light-Induced Conformational Changes of the AppA BLUF Photoreceptor
In 2007 KP worked at Utrecht University as Young Guest Researcher. She worked on the AppA BLUF
Photoreceptor light induced conformational changes. During 2007 KP learned expression and purification of
recombinant proteins. She produced the BLUF domain and characterized it by NMR.
In 2008 KP won a grant from the Stichting Magnetische Resonantie. In this period she performed the
characterization of the BLUF conformational changes through a combination of NMR and docking
techniques.
Udine University
Dialysis related amyloidosis
In 2008-2009 she had a Post Doc position at the Udine University, studing dialysis related amyloidosis.
Amyloidosis associated with long term hemodialysis results from the deposition of β2-microglobulin (b2m).
To this day the onset of this amyloidosis can be delayed but not avoided in dialysis-related amyloidosis
patients.
During this Post Doc period she addressed the following topics:
-study of the interaction between b2m and Camelidae nanobodies specifically designed to interact with b2m,
with the aim of identify nanobodies able to inhibit the fibrillogenesis and use them in diagnosis and as
therapeutics;
-interaction between b2m and doxycycline, a antibiotic from tetracyclines family. Demonstration of the
capability of the antibiotic to stop the misfolding process of b2m.
National Council of Research, Institute for Macromolecular Studies, Milan
From October 2009-today KP is Post Doc at ISMAC-CNR in Milan working on the following projects:
-study of the molecular mechanism of inhibition of the fibroblast growth factor 2 (FGF2) proangiogenic
activity by an angiostatic small molecule that mimics the endogenous inhibitor of angiogenesis,
thrombospondin-1;
-investigation of PTX3 derived antiangiogenic lead for its binding to FGFs/FGFR system involved in tumor
growth and angiogenesis;
-use of a bile acid binding protein as host for xanthene dyes for the development of new bio-optoelectronic
devices;
-N-alkylated indanylidenepyrroline (NAIP) Schiff base: caging of the biomimetic dipolar photoswich into
BABP protein for the achievement of new functional materials;
-development of sensors for Alzheimer biomarkers diagnosis;
-exploration of the binding potential of Ferritin for natural lipids and synthetic derivatives.
Teaching Experience:
2008-2009 She taught Molecular modelling within the module Structural Proteomics and Molecular Modelling
for the Degree Course "Biotechnologies", Udine University.
2005-2008 She taught Nuclear Magnetic Resonance Spectroscopy, theory and practice within the course of
"Phisics" for the First Degree Course in "Biotechnologies", Udine University.
2011 She gave a lecture on "Protein-protein and protein-ligand interaction studies by Nuclear Magnetic
Resonance spectroscopy" within the Molecular Medicine PhD Course, Milano University.
Publications in peer-reviewed journals:
1. Tomaselli S*, Giovanella U*, Pagano K*, Leone G, Zanzoni S, Assfalg M, Meinardi F, Molinari H, Botta C,
Ragona L "Encapsulation of a rhodamine dye within a bile acid binding protein: toward water processable
functional bio host-guest materials" Biomacromolecules. 14(10):3549-56 (2013) (*These authors
contributed equally)
2. Pagano K, Tomaselli S, Zanzoni S, Assfalg M, Molinari H, Ragona L "Bile acid binding protein: a versatile
host of small hydrophobic ligands for applications in the fields of MRI contrast agents and bionanomaterials" Computational and Structural Biotechnology Journal. Volume No: 6, Issue: 7,
e201303021 (2013)
3. Pagano K, Torella R, Foglieni C, Bugatti A, Tomaselli S, Zetta L, Presta M, Rusnati M, Taraboletti G,
Colombo G, Ragona L "Direct and allosteric inhibition of the FGF2/HSPGs/FGFR1 ternary complex
formation by an antiangiogenic thrombospondin-1-mimic small molecule" PLoS One. 7(5): e36990 (2012)
4. Tomaselli S, Assfalg M, Pagano K, Cogliati C, Zanzoni S, Molinari H, Ragona L "A disulfide bridge allows
for site-selective binding in liver bile acid binding protein thereby stabilising the orientation of key amino
acid side chains" Chemistry. 19(13):4092 (2012)
5. Giorgetti S, Raimondi S, Pagano K, Relini A, Bucciantini M, Corazza A, Fogolari F, Codutti L, Salmona
M, Mangione P, Colombo L, De Luigi A, Porcari R, Gliozzi A, Stefani M, Esposito G, Bellotti V, Stoppini M
"Effect of tetracyclines on the dynamics of formation and destructuration of beta2-microglobulin amyloid
fibrils" J Biol Chem. 286(3):2121-31 (2011)
6. Pagano K, Bemporad F, Chiti F, Fogolari F, Viglino P, Esposito G, Corazza A “Structural and dynamics
evidences of Sulfolobus solfataricus Acylphosphatase oligomeric species” J Biol Chem 285(19):14689700 (2010)
7. Pagano K, Fogolari F, Corazza A, Viglino P, Esposito G "Estimation of 3J_HN-Halpha and 3J_HalphaHbeta coupling constants from heteronuclear TOCSY spectra" J. Biomol. NMR. 39: 213-22 (2007)
8. Pagano K, Ramazzotti M, Viglino P, Esposito G, Degl'Innocenti D, Taddei N, Corazza A “NMR solution
structure of the Acylphosphatase from Eschaerichia coli” J. Biomol. NMR. 36: 199-204 (2006)
9. Corazza A, Rosano C, Pagano K, Alverdi V, Esposito G, Capanni C, Bemporad F, Plakoutsi G, Stefani
M, Chiti F, Zuccotti S, Bolognesi M, Viglino P "Structure, Conformational Stability, and Enzymatic
Properties of Acylphosphatase From the Hyperthermophile Sulfolobus solfataricus" Proteins. 62: 64-79
(2006)
10. Schievano E, Pagano K, Mammi S, Peggion E “Conformational Studies of Aib-Rich Peptides Containing
Lactam-Bridged Side-Chains: Evidence of 310-Helix Formation.” Biopolymers. 80: 294-302 (2005)
Conferences, symposia and workshops with ISSN or ISBN number:
1. Speranza G, Ambrosini S, Bagnasco L, Bavaro T, Cosulich E, Francescato P, Lesma G, Marrubini G,
Massolini G, Meregaglia A, Morelli C F, Pagano K, Pappalardo, V, Pedrali A, Ragona L, Serra I, Silvani
A, Terreni M, Tomaselli S, Torres-Salas P, Ubiali D, Vece V (2014). Lino e canapa: una fonte preziosa di
nuovi prodotti ad alto valore aggiunto. In: Progetto VeLiCa Da antiche colture materiali e prodotti per il
futuro, ISBN/ISSN: 978-88-907569-1-7
2. Foglieni C, Torella R, Bugatti A, Pagano K, Ragona L, Ribatti D, Rusnati M, Presta M, Giavazzi R,
Colombo G, Taraboletti G (2012). Inhibition of FGF-2 angiogenic activity by novel small molecules
mimetic of thrombospondin-1 (TSP-1). THROMBOSIS RESEARCH, vol. 129; p. S193-S193, ISSN: 00493848
3. Pagano K, Corazza A, Fogolari F, Viglino P, Giorgetti S, Raimondi S, Stoppini M, Bellotti V, Esposito G
(2010). Doxycycline affects association and folding of beta 2-microglobulin. AMYLOID, vol. 17; p. 93-93,
ISSN: 1350-6129
4. Schievano E, Pagano K, Mammi S, Peggion E, BE Chorev M, Sawyer TK (2004). 3(10)-helix in Aib-rich
peptides containing lactam-bridged side-chains: Spectroscopic characterization in TFE by CD and NMR.
BIOTECHNIQUES; p. 375-376, ISSN: 0736-6205
5. Schievano E, Pagano K, Mammi S, Peggion E (2003). 3(10)-helix in Aib-rich peptides containing lactambridged side chains: Spectroscopic characterization in TFE by CD and NMR. PEPTIDE SCIENCES, vol.
71; p. 326-326, ISSN: 0006-3525