Meeting schedule
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Wednesday, Feb. 10 |
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Thursday, Feb. 11 |
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Friday, Feb. 12 |
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09:00 |
R. Subirós-Funosas |
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09:00 |
M. Morais |
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09:20 |
T. Esteves |
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09:20 |
B. De la Torre |
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09:40 |
I. Güell |
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09:40 |
K. Scherer |
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10:00 |
M. Melo |
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10:00 |
A. Melo |
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10:20 |
G. Fuertes |
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10:20 |
M. F. Palomares-Jeréz |
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10:40 |
Coffee break |
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10:40 |
Coffee break |
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11:10 |
N. Aguiam |
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11:10 |
M. Monsó |
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11:30 |
A. Diez-Torrubia |
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11:30 |
C. Ciobanasu |
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11:50 |
M. Bastos |
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11:50 |
P. Borrego |
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12:10 |
C. Junkes |
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12:10 |
P. Matos |
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12:30 |
M. Domingues |
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12:30 |
H. Franquelim |
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12:50 |
Lunch |
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12:50 |
Lunch |
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14:00 |
Registration |
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15:00 |
A. Afonso |
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15:00 |
R. Tapia |
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15:20 |
P. Sánchez-Murcia |
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15:20 |
Y. Palacios-Rodríguez |
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15:40 |
R. Halai |
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15:40 |
W. Kowalczyk |
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16:00 |
V. Teixeira |
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16:00 |
Y. Mirassou |
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16:20 |
F. Carvalho |
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16:20 |
C. Alves |
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16:15 |
Welcome reception |
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16:40 |
Coffee break |
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16:40 |
Coffee break |
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17:00 |
Plenary
lecture 1
Rein Ulijn |
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17:10 |
P. Ruiz-Sanchis |
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17:10 |
M. Bagheri |
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17:30 |
P. Ventosa-Andrés |
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17:30 |
A. Diaz-Cirac |
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17:50 |
D. Nuñez-Villanueva |
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17:50 |
M. I. Carcía-Aranda |
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18:10 |
Plenary lecture 2
David Craik |
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18:10 |
M. Sanchez |
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18:10 |
R. Prades |
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18:30 |
I. Alves |
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18:30 |
M. Ribeiro |
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20:30 |
Closing dinner |
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Chairman |
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Session |
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D. Andreu |
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Feb 12,
17:50-18:40 |
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E. Bardají |
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Feb 12,
11:10-12:50 |
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E. Giralt |
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Feb 11,
9:00-10:40 |
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F. Albericio |
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Feb 11,
15:00-16:40 |
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H. Maia |
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Feb 10,
17:00-18:50 |
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J. L. Mascareñas |
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Feb 11,
17:10-18:50 |
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J. Villalaín |
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Feb 12,
15:00-16:40 |
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M. Prieto |
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Feb 12,
9:00-10:40 |
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N. Santos |
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Feb 12,
17:10-17:50 |
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P. Gomes |
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Feb 11,
11:10-12:50 |
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KEYNOTE SPEAKERS
The XII EPI will have the presence of two keynote
speakers that embody the eclectic “peptides across
disciplines” spirit.
Dr.
David Craik leads the NMR and protein structure in
drug design group at the University of Queensland
(Brisbane, Australia), which uses NMR spectroscopy
to determine the structures of proteins that are
important in drug-design programs and in
agriculture. By elucidating the structures of
biologically-active proteins they are able to
identify regions crucial for activity and can use
this information to design new drugs. The proteins
they study come from a range of animal and plant
sources but are often involved in host defence.
Examples include the conotoxins (venom components
from marine snails) and the cyclotides (novel
circular proteins from plants). Find out more at
Craik’s website (http://www.imb.uq.edu.au/index.html?id=11695).
The
work of Dr Rein Ulijn’s group is focused on the
development of new synthetic materials and systems
that are inspired by biology and have unique
properties, such as adaptability, molecular
recognition and programmability. These properties
open up exciting new applications in wide ranging
areas ranging from biomedicine to nanotechnology.
Among the most meaningful studies being carried out
are:
1) Peptide nanomaterials via self-assembly. A new
molecular architecture for self-assembled hydrogels
of aromatic short peptide derivatives, forming
nanoscale fibres, hollow tubes or sheets, depending
on the amino acid sequence, was proposed. 2)
Enzyme Assisted Self-Assembly In this approach,
molecular self-assembly provides a thermodynamic
driving force that enables a protease to produce
building blocks in a reversible and spatially
confined manner. 3) Enzyme-responsive materials.
Enzyme-responsive materials (ERMs) are a new class
of smart materials that undergo macroscopic
transitions when triggered by selective catalytic
actions of enzymes with applications in diagnostics
and controlled release. 4) Nano/Biointerface.
This area relates to the design of active and
dynamic interfaces between biomolecules and
synthetic functional materials. Find out more at
Ulijn’s website (
http://www.ulijnlab.com )
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