Bioinspired nanomaterials

Transcription

Bioinspired nanomaterials
Johannes Raff
nanoSeminar
Institute of Materials Sciences
11.11.2010
Institute of Radiochemistry y www.fzd.de y Member of the Leibniz Association
Outline
• Forschungszentrum Dresden-Rossendorf
• Institute of Radiochemistry
• Microbe radionuclide interaction
• Bacterial S-layers
• Metall binding by bacterial S-layers
• Application potential of bacterial S-layers
• S-layer based materials
• Biomass productions
• Summary
• Future cooperation IRC-FZD with IfWW-TUD
Institute of Radiochemistry y Dr. Johannes Raff y www.fzd.de y Member of the Leibniz Association
Forschungszentrum Dresden-Rossendorf e.V. (FZD)
As of 01.01.2011
Ion-Beam Center
Ion-Beam Physics and Materials
Research
Advanced Materials
Radiation Physics
Radiochemistry
Cancer Research
Radiopharmacy
Nuclear Safety
Research
Safety Research
High Magnetic Field Laboratory
Radiation Source ELBE
Rossendorf Beamline
(ESRF, Grenoble)
PET-Center
TOPFLOW-Facility
Dresden High Magnetic
Field Laboratory
I FZD: Facts and figures
• Member of the Leibniz-Association
Change to the Helmholtz Association
as of 01.01.2011, as HZDR
(Result of the evaluation 2007)
• Foundation:
01.01.1992 (e.V.)
• Employees:
~ 800 total (incl. PhD, Annex, projects, trainees)
~ 400 basic funding
~ 370 scientists
• Budget 2009:
~ 60 Mio € basic funding
~ 20 Mio € third party funding
Institute of Radiochemistry
Dresden
Radiochemical lab building 8b
Office and lab building 8a
Micobiological and radiochemical labs,
Divisions Biogeochemistry, Surface Processes, Biophysics
Leipzig
Radiochemical laborytories
FZD research site Leipzig, Division Reactive Transport
Grenoble
ESRF Beamline ROBL, France
Division Molecular Structures
I Research at the Institute of Radiochemistry
Radio-ecological research on the behaviour of actinides in nature
Long term disposal
of radioactive waste
Fungi
Humans
Meat
Milk
Fruits
Animals
Bacteria
Fungi
Water
Bread
Grain
Plants
Soil
Air
Soil
Water
Algae/plants
II Sources of radioactive heavy metals (uranium)
Natural and anthropogen sources of actinides and radionuclides
Reprocessing plants
Uranium deposits and minerals
Nuclear power plants
Storage tanks
Nuclear warhead, USA
Uranium mining waste piles
Nuclear
explosions
Phosphate fertilizer
Uranium
ammunition
Storage
Cement production
Our aim: protect people and environment from being affected by actinides
Fundamental research
Microbe radionuclide interaction
Uranium mining waste pile
“Haberland” nearby Johanngeorgenstadt, Saxony
Biosorption
Uptake
Complexation
Biotransformation
- Determination of
the microbial
diversity via gen
analysis
- Isolation of
bacteria
Research on the interaction
of actinides with
microorganisms
Biomineralization
Bacterial S-layers
Interesting
properties of S-layer
Heavy
metals
Paracrystalline
protein
envelope
(S-layer)
☺
☺ ☺
- Self assembling
proteins
- Multifunctional
- Intelligent interface
to the bacterial
environment
- Metall binding
- Some with high
stability
☺
☺
☺
Trace
elements
Cell wall
I Identified isolates with S-layer proteins (16S rRNA gene analyses)
JG-B7
Lysinibacillus fusiformis SW-B9 (AY907676)
Lysinibacillus sphaericus DSM28T (AJ310084)
Fundamental
research
Application oriented research
Lysinibacillus sphaericus JG-A12
JG-B53
JG-B62
JG-B58
Bacillus psychroviridis 433-D9 (AY266991)
JG-B5T
Bacillus pumilus Tbl (AB195283)
JG-B12
JG-B35
JG-B37
JG-B41
Bacillus cereus AH 521 (AF290554)
Bacillus mycoides ATCC6462 (AB021192)
Bacillus weihenstephanensis DSM118221 (AB021199)
0.01
Total 144
Bacillus/Lysinibacillus
isolates
Metal binding by bacterial S-layers
Molecular
biology
Spectroscopy
XAS
Elements
ICP-MS
N/R
ATR-FTIR
Microscopy
TRLFS
χ(k)k
3
I EXAFS investigations of formed uranium protein complexes at pH 4,5
L. sphaericus JG-A12 S-layer
L. sphaericus JG-A12 spores
2
4
6
8
-1
k[Å]
10
12
Fourier Transform Magnitude
L. sphaericusJG-A12 cells
Oax: 1.77 Å
Oeq1: 2.31 Å
Oeq2: 2.45
ÅC: 2.88 Å
P: 3.61 Å
P
C
Oeq1
0
U
Data
Fit
C
0
2
4
R + Δ [Å]
6
8
U Oeq2
P
Used model for the fit
of the uranium spectra
(parts of two molecules, meta-autunite and
uranyltriacetate).
Merroun, M.et al.(2005) Appl. Environ. Microbiol. 71(9): 5532-5543
Raff, J. et al. (2004) In Water-Rock Interaction, Richard B. Wanty und Robert R. Seal II, A.A. Balkema Publishers, New York, p 97-701
1544
PO4 ?
924
1165
1238
1398
νas(UO22+) bidentate binding by COOH
1456
1636
II ATR-FT-IR investigations of formed uranium protein complexes at pH 4
JG -A12
N C T C 9602
Absorption
Absorption
D S M 2898
A12
1078
JG -B 7
1033
B62
JG -7B
JG -B62
JG -B 58
1800
1600
1400
1200
W avenum ber / cm
1000
-1
800
B58
1140
1120
1100
1080
1060
1040
1020
-1
Wavenumber / cm
1000
980
960
III Supporting EXAFS/IR investigations using poly-Glu and Phosvitin, pH 4
10
Denatured
phosvitin with
PbCl
0
FT
-5
2
ax
2
S-layer B62 + 0,1 mM U
4
6
S-layer B62 + 1 mM U
1.0
0.5
Phosvitin + 0,1 mM U
0.0
Phosvitin + 1 mM U
8 10 12 14 16
-1
k [Å ]
0 1 2 3 4 5 6
R + Δ [Å]
Polyglutamate
alpha carboxyl
1083
Absorption
Wavenumber / cm
Feldman-Complex
2.41Å
-4
10 M
-3
10 M
1800
1600
1400
1200
1000
800
-1
wavenumber / cm
2.34Å
Denatured
phosvitin with
800 10-3 M U(VI)
Li, B. et al.(2010) J Inorg Biochem 104(7), 718-725
ax -U
1 -O
UO
Uranyltriacetate
3.76Å
1000
-1
5
Denatured
phosvitin with
10-4 M U(VI)
dis
1.5
1456
2+
U-C
dis
U-C-C
dis
U-C-C -C
923
1200
Poly-Glu 1 mM U
Oeq1
Oeq2
C
1016
1400
2.5
2.0
1096
1600
15
1022
1800
Poly-Glu 0,1 mM U
1410
9.8:1
3.0
1539
f
925
1019
1:1.02
20
Denatured
phosvitin from
saturation
UO2
U:P
25
4.0
3.5
1716 -COOH
918
1027
d
ax
4.5
1531
b
O
30
1652
Phosvitin
Solution
5.0
χ(k)*k
3
1001
1085
930
1078
1180
1228
1400
1465
Absorption
a
e
exp.
fit
35
1540
1655
Phosvitin
IV P/S-K edge XANES measurements
P K-edge XANES
S K-edge XANES
S-layer
S-layer
S-layer + U(VI)
S-layer + U(VI)
S-layer
S-layer
S-layer + U(VI)
S-layer + U(VI)
No evidence, that Phosphate groups are not involved in the U(VI) binding,
but sulfur-species interact also.
Sulfoxide
at 2474.9 eV
and
sulfate
at 2483.8 eV
JG-B58
JG-B12
JG-B5T
JG-B62
JG-B7
JG-A12
Glycoproteins
V Posttranslational modifications of the S-layer proteins: glycosylation
Detection of glycosylated
proteins by means of the
“DIG glycan detection kit”.
Dark bands indicate glycosylation.
Absorption
maxima
Sugar
residue
(nm)
(mol/mol)
JG-A12
-
0,03
JG-B5T
477
2,46
JG-B7
482
1,93
JG-B12
482
4,74
JG-B58
477
2,33
JG-B62
482-485
3,79
S-layer
Modified colorimetric determination of
sugars after Dubois.
Weinert, U. et al.(2010) Anal Biochem (in preparation)
VI Limited proteolysis for the localisation of the posttranslational modifications
Proteolytic digestion of native S-layers from L. sphaericus JG-A12 and NCTC 9602
using the endoproteinase Glu-C (–Glu-P1´– and –Asp-P1 – in Phosphate buffer)
JG-A12
JG-A12
9602
MANQPKKYKKFVATAATATLVASAIVPVASAAGFSDVAGNDHEVAINALADAGIINGYADGSFKPNQTIN
RGQVVKLLGRYLEAQGQEIPADWNSKQRFNDLPVTAEEELVKYAALAKDAGVFNGSNGNLNASQTMQRQQ
MAVVLVRAIKEIAGVDLVAEYKKANFVTEIGDLDKAYSAEQRTAIVALEYAGITNVAHFNPGNSVTRGQF
ASFLYRTIENVVNNPEAGVAAVKAINNTTVEVTFDEEVDNVQALNFLISDLEVKNAAVKLTNKKVVVLTT
AAQTADKEYTVSLGEEKIGTFKGIAAVVPTKVDLVEKSVQGKLGQQVTLKAQVTVAEGQTKAGIPVTFFI
PGSANGVKTPVTVEAVTNEEGIATYSYTRYAATNDTVTVYANGDRSKFSTGYVFWAVDQTLEITEVTTGA
TINNGANKTYKVTYKHPETGKPVSGKVLNVSVKENIDVTVDKLQNVTVNGIAVVQTSDNNTRAAQITTDS
KGEATFTVSGSNAEVTPVVFEATPVQVTNTNGAVTTTSYTQKYTADILQASAAKVTFGAVQAAYTLEVTR
DGGEVAATGVENGRKYNLVVKDKDGKLAANETVNVAFNEDIDGVISTVTSAEFVKVENDKQVRYEGKKIT
VKTNSKGEASFVISSEAVNTYATPIAWIDINNQSAKDANLDKGEPSAVAPISYFQAEYLDGSKLVSYKDT
TETDKFTGSETATFKVQLTNQSGKVVKNSGYTTPNVSYTVYNTGANNVKVDGVEIAPNRVHTVVAKDGVI
NVTTVDNKSSSVKVLATGVAKQTNGNKEFAFTSKEATATFTATNEVSNPYTGAVKHYNTDKKTITFDNKD
AIKYAGVKGKTYKYFGLGSTPIANADAFIATLSGQGAGNQVTVTYKEEDDVVSFYIISVVNGGIGNPTTD
PALANGVTGTIAFTNTSFNASANQTITVKDADLNVNATVADTTTVTITDSAKTTFNITLTETGVNTGEFT
GTLTSAQLALLKDGVITATYNDAKNANNVAATATATATLNTTVGAVNFAAKATTEYSEGVGTAAKVEGST
VLTSKVDTGDLVLVVDGVQFTTVVTAIDPGTSATASLTAVVAEINAAAKKVGFTADVATVDADKIVLTSP
TKGTSSSVEVKDLGTTTGLGLTKAPEVKGTAGAAVATQWKFTVTTTPAVGETITVKVGTKEASHKVVAGN
DLAAIATALNTAIGADYNIALVTGSNVITVTQATPAKTTDELSVTVTK
9602
MANQPKKYKKFVATAATATLVASAIVPVASAAGFSDVAGNDHEVAINALADAGIINGYADGSFKPNQTIN
RGQVVKLLGRYLEAQGQEIPADWNSKQRFNDLPVTAEEELVKYAALAKDAGVFNGSNGNLNASQTMPRQQ
MAVVLVRAIKEIAGVDLVAEYKKANFVTEIGDLDKAYSAEQRTAIVALEYAGITNVAHFNPGNSVTRGQF
ASFLYRTIENVVNAPEAGAAAVKAVNNTTVEVTFDEEVDNVQALNFLISDLEVKNAAVKQTNKKVVVLTT
APQTADKEYTVSLGEEKIGTFKGIAAVVPTKVDLVEKSVQGKLGQQVTLKAQVTVAEGQTKAGIPVTFFI
PGSANGVKSPVTVEAVTDENGVASYTYTRYAATNDTVTVYANGDRSKFSTGYVFWAVDTTLEITEVTTGD
IINNGANKTYKVAYKDPETGKPVSGKVLNVSVKENIDVTVDKLQNVTINGIKVAQTSTSNTTAAQVTTDS
KGEATFTITGANAEVTPVVFAGEAVTGQTLPSQKYNADALQTTAKKVKFGALQADYILEVTRDGGETAAT
GYDNGRKYKLVVKDKNGKLAANETVNVAFNEDIDGVISTTTDAKFVKLDNEDNQVGWDTTVDKDAKKITV
KTDSKGEASFIIGNTKENTYYTPIAWIDVNYQSGKVGTLDQGEPSATAPISYFQSPTIDGSKLVAENKDG
KKPSDFEDKDAIFKVVLVNQSGKEMKNHNYKTEKVSYTVNNTGSNEAVVEYTYNGKVESETLAPNRATSV
VADNGTITVKPNGKTTSVKVLATGVAKEDKTNGKEYAFTAKEATAKFTATKEISNPYTGAIKYYDTDKKT
ITFDGKDAIKYAGESGKKYKYYSGNIEVATEKAFIDLLANASGKVTVTYKVEDDTKSFHIINVGTDVANK
PVEKKDDTKPTNNAPVAKQVADQVIASNGSKLTFTANDVASDADKDTLKIVTAYTTNSTVATATTDANQL
GFSVEPKGEGSTTVTVVVTDGKDNINVSFKVNVSTASYTSVVNSGNPVKDFAPAVPTAATAKLPEFTSVA
KAGTIKVQGFDIPLTLGSTQAQVLETLNNFITDYKINASAKLVDKAIVISSTETGNAATLTVEGDSTLEL
VAGTVLGTVSTTPGSVGTATPAKYAVKVLNGVSNGTKVDFKFTIGAKTVTVTVDATAGAKAVSDVVDTLA
AATLDGYSITKNGDVIELTQTTPATTTDKLVVETKKAN
VII Posttranslational modifications of S-layer proteins: phosphorylation
Proteolytic digestions of native S-layer endoproteinase Glu-C
M
1
2
3
4
5
*
*
*
*
*
*
*
*
Samples
M: Marker
1: S-layer JG-A12
2: S-layer NCTC 9602
3: Glu-C digested JG-A12 SL
4: Glu-C digested 9602 SL
5: Phosvitin
P-positive references in lane…
M: Ovalbumine 1,73 P:1 (0.12 %)
5: Phosvitin 100 P:1 (10 %)
P-positive bands are indicated by
an asterix
Stains-all staining
N-terminal sequencing of the fragments
VIII Sequence analyses and localisation of the modified amino acids
0
Signal sequence
L. sphaericus JG-A12
820 aa
210 aa
1207 aa
Phosphorylation
N-terminal
domain
Central domain
C-terminal
domain
1197 aa
L. sphaericus 9602
Phosphorylation
Glu-C cleaving sites in the native protein;
theoretical 125 (JG-A12) and 141 (9602)
Possible sites.
C-terminus
S-layer
P
N-terminaler
anchor
Cell wall
Pollmann, K. et al. (2005) Microbiology, 151(9): 2961-2973
IX Hypothesis: phosphorylated amiono acids mediate the release of S-layers
Uranium
COOHgroups
bind uranium
Uranium mining
waste pile
isolate
Signal transduction
???
Expression of
new S-layer
proteins
S-layer
gene
Formation of a
new S-layer
Secretion of
the protein
monomers
Release of the uranium
saturated S-layers
- phosphate group(s)
as a switch?
- role of sulfurspecies?
X Investigation of the hierarchic organisation of S-layer proteins
pH
Monomers (%)
Hypothesis:
9
8
7
6
5
4
3
25
9
9
16
17
60
100
- Me2+
- Me2+
Me2+
Me2+
(5 mg/ml S-layer JG-A12,
0.1 M NaCl)
- Me2+
Me2+
Me2+
Me2+
2+
Me2+ Me2+ Me
Application oriented research
Application potential of bacterial S-layers
Some natural functions
Applications
Extreme
environments
Functional
diversity of the
S-layer
Diversity
of possible
technical
materials
Biosensoren
Pollmann, K. et al. (2006) Biotechnology Advances 24 (1), 58-68
S-layer based materials
Bacterial
waste pile
isolates
S-layer isolation
Intact polymers
Monomer
solution
Sol-gel
embedding
(particles or
coatings)
Production
of S-layer
covered
Controlled recrystallization direct on
hollow
carriers or after activation
spheres
I S-layer coatings with polyelectrolyte support
•
•
•
To improve the surface properties for S-layer recrystallization a polyelectrolyte interface
can be introduced
Simple LbL-coating
Layer composition influences the stability of the protein coating
Modified after Decher, G. SCIENCE 277(5330), 1232-1237
Without polyelectrolyte support
- Recrystallization on
SiO2
- 57 % coverage
- 12 h incubation
with polyelectrolyte support
- Recrystallization on PEcoated Si
- >90 % coverage
- < 30 min incubation
- Monolayer
II S-layer coated polyelectrolyte hollow sheres
•
Coating of spheric
templates (CaCO3, CaP)
with multiple layers (410-…) of polyelectrolytes (PSS, PAH)
•
Dissolution of the core
material by HCl
•
Coating of the spheres
with S-layer(s) via
recrystallisation and
LbL-techniques
•
Mono- or multifunctional
transparent speres
• Magnetic “beads”
• Combination of
binding molecules
and catalysts
• …
III Functionalization of S-layer coatings
Multifunctional
multi layer systems
Metal
binding
Production of
nano-particles
Dyes
Enzymes
Aptamers
Antibodies
PEL
PEL
Possible carrier materials:
Glas
Ceramics
Metal
Plastics
IV Metal/metalloid filters
Water
Dissol
ved me
tal ions
Selective binding
Advantages compared to previous approaches:
- Binding properties
- Environmental-friendly disposal
- Selectivity ?
http://www.periodictable.com
Raff, J. et al. (2003) Chem Mater 15(1): 240-244
Institute of Radiochemistry y Dr. Johannes Raff y www.fzd.de y Member of the Leibniz AssociationPatent
DE 101 46 375
V Uranium binding by cells and S-layer proteins
19,5
S-layer
64,0
92,5
JG-B62
Cells
76,6
411,7
JG-B58
Isolates
JG-B53
JG-B41
JG-B37
99,9
31,6
33,3
JG-B35
JG-B5T
49,1
11,6
350
150,0
149,2
144,2
143,3
JG-B12
JG-B7
157,4
42,5
291,5
182,5
168,3
229,1
Bound uranium (in mg U/g dw)
Uranium binding
(in µg U/mg dry weight)
JG-A12
JG-B7
DSM 2898
JG-A12
NCTC 9602
Cells
S-layer
300
250
200
150
100
50
0
4
5
6
7
8
pH
Raff, J., Selenska-Pobell, S. (2006) NEI 51 (619) 34-36
VI Arsenic binding by cells and S-layer proteins
580
Project:
600
BIO MATUM
living
dead
2000
100
Bound As(V) (in µg/g)
171
117
179
332
182
140
133
117
200
266
289
300
328
400
269
1500
1000
500
rp
Fe
rr
o
so
-B
62
53
JG
-B
JG
-A
12
7
JG
-B
02
N
C
JG
96
TC
13
24
0
0
98
Z
TC
SM
D
ce
A
en
er
C
12
98
1
Z
28
EM
rs
ls
ef
SM
ye
el
As(V) bindung by living and dead
biomass, using a As(V) solution with
[As] = 10 mg/l
R
ae ica nis cus um cus orp
g
in uth mu eni teri eri ros
r
a ha
er
sy lym om ars
g
.
F
p
e s
P .p
. c B.
M
. m L.
S
B
C
0
la
S-
0
D
Bound As(V)
[µg/g dry biomass]
500
As(V) bindung by cells and S-layers of
reference strains and uranium mining
waste pile isolates, using a As(V)
solution with [As] = 10 mg/l
Reference material: Ferrosorp (granulated ferric hydroxide)
Matys, S. et al. (2010) FZD-Report 530
VII Pt and Pd binding by S-layer
1900
JG-B35
924
1800
JG-B41
825
Isolate
490
JG-B7
710
JG-A12
1147
815
JG-B53
JG-B62
820
1023
235
760
Bound metal (in mg Me/g dry weight)
Pt
Pd
Fahmy, K. et al. (2006) Biophysical Journal 91 (3), 996-1007
VIII Removal of contaminants or recovery of resources
Rain
Dissolved
metals/
metalloids
Former
mining sites
Metal removal
or recovery
River,
lakes,
sea
Geogenic
deposits
Industry
IX Metal/metal oxide catalysts
Incubation with a metal salt
soultion
+ Addition of
reducing /
precipitation
agents
Defined catalytic active nanoparticles e.g.
Pt, Pd, Fe/Pd, Fe/Pt
ZnO, TiO2
with sizes of 1-26 nm
X S-layer based synthesis of defined and regular arranged nanoparticles
Adding
metal
salt
solution
Adding reducing
reagents
Protein
removal
via UV
XI Synthesis of Pt nanoparticles on different coatings
Protein removed by UV
Nanoparticles produced on
PE without S-layer
Protein removed by UV
Nanoparticles produced on
PE + S-layer
XII Precious metal catalysts for the synthesis of defined CNT´s
Possibly migration and agglomeration of the particles
Further improvement necessary
XIII Photocatalytic active coatings for the degradation of pharmaceuticals
Projects:
t
gh
Li
Inorganic
degradation
products
NanoAqua
Water
Pharm
aceutic
als
ZnO or TiO2 nano-particles
- Environmental-friendly (disposal, immobilization of
nano-particles)
- Higher efficency (required energy, day light sensitivity) ?
Patent pending
XIV ZnO based photocatalysts for the elimination of pharmazeutica
A
100
Intensity (cps)
cDiclofenac [µM]
(0 0 4)
(2 0 0)
(2 -1 2)
(2 0 1)
100
(1 0 3)
(2 -1 0)
(1 0 2)
(0 0 2)
(1 0 1)
(1 0 0)
80
60
40
20
0
80
0
5
10
15
20
25
t [h]
60
40
Z pH 7,3 + JG-B53
Z pH 8,3 + JG-B53
Z pH 9,0 + JG-B53
Z pH 7,3 + JG-A12
Z pH 8,4 + JG-A12
Blindwert
B
20
100
0
40
50
60
70
Scattering angle (deg)
Top: XRD-pattern of S-layer supported ZnO (red
graph) and equally prepared ZnO without protein
(green graph). S-layer prepared ZnO-particles
have a size of about 14 nm.
Right: Diclofenac elimination by S-layer supported
ZnO in suspension (A) and immobilized on a
carrier (B).
c Diclofenac [µM]
90
30
80
70
60
50
0
5
10
t [h]
T + PEM + Z pH 8
T + PEM + JG-A12 + Z pH 8
Blindwert
15
20
T + PEM + Z pH 9
T + PEM + JG-B53 + Z pH 8
25
XV Photocatalytic elimination of pharamceuticals in water
Manufacturer
Hospitals
Product path
Private
households
Animal
husbandry
Photocatalytic
treatment
Water path
River,
lakes,
sea
Dumps
Wastewater
treatment plants
XVI Sensory coatings for the detection of pharmaceuticals
Project:
AptaSens
FRET
Acceptor
Donor
Aptamer
Organic compound e.g
pharmaceutical
- Transferability
- Chip-based quantification of several analytes ?
- lower unspecific binding ?
Patent pending
XVII S-layer bound fluorescence dyes and aptamers
FRET-pair
a)
c)
b)
S-layer aptamer composite
d)
f)
e)
Thrombin binding by the S-layer bound aptamers (IAsys)
100 µg
Biomass production
Process
Yield in g/l
(z.B. JG A12)
Biomass
S-layer
Manpower
requirements
Conventional
3
0,03
6,9
19000
Pilot plant
6
0,16
1,4
730
Optimisation
12
0,85
1,4
100
Aim
Possible strategies:
€/g
S-layer
- High density cultivation
- Heterologous expression
<10
Summary
• S-layers are essential for many bacteria to survive in extreme
environments.
• S-layer proteins are highly complex proteins with many different
functional groups and modifications, directly affecting their molecular
behavior (conformation, hierarchic organization, metal binding).
• Their metal binding and self-assembly properties make S-layers very
worthwhile for the development of new materials for
• environmental techniques
• biotechnology
• nanotechnology,
but for their application we need to know more about them.
Future cooperation IRC-FZD with IfWW-TUD
• Submitted EU-project “ActiveBrane”
Development of reactive nanomembranes with low
biofouling for decomposition of organic pollutants in
water streams by applying a novel sandwich technology
• Arsenic binding by S-layers
Planned DFG project
Arsenic binding aptamers
• Aptamer based sensors for different pollutants
Planned project
Acknowledgement
Research:
Co-operation partners:
Ulrike Weinert
Franziska Lederer
Tobias Günther
Anne Heller
Bo Li
Manja Vogel
5 Institutes
André Marquard
Falk Lehmann
Tobias Hauptmann
Dr. Sabine Kutschke
Dr. Katrin Pollmann
Dr. Harald Foerstendorf
Dr. Henry Moll
Dr. André Rossberg
Presented work was funded by:
Dr. Sabine Matys (IfWW)
Dr. Ulrich Soltmann (GMBU)
Dr. Mohamed Merroun
(Universität Granada, Spanien)
350
JG-B7
DSM 2898
JG-A12
NCTC 9602
Cells
S-layer
300
250
200
150
100
50
0
4
5
6
7
8

Bioinspired nanomaterials

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