DTIC ADA462845: Rapid, Room-Temperature Formation of Crystalline Calcium Molybdate Phosphor Microparticles via Peptide-Induced Precipitation

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DOI:10.1002/adma.200600243 U
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Rapid, Room-Temperature Formation of Crystalline Calcium IC
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Molybdate Phosphor Microparticles via Peptide-Induced T
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Precipitation**
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ByGul Ahmad,Matthew B. Dickerson,Benjamin C. Church,Ye Cai,Sharon E. Jones,Rajesh R. Naik,
Jeffrey S. King,Christopher J. Summers,Nils Kröger,andKenneth H. Sandhage*
Nature provides numerous examples of organisms that emitting phosphors stimulated by light-emitting diodes for
synthesizeintricate mineralstructures(biominerals)with mi- lightingapplications),[4]ascatalystsinpetrochemicalprocess-
cro-tonanoscalefeaturesthroughtheuseofspecificbiomole- ing (e.g., as an ester-exchange copolymerization catalyst),[5]
cules.[1] While such control over mineral formation under andasnontoxiccorrosion-inhibitingpigments(e.g.,forpaints
ambientconditionsexceedscurrentman-madeassemblytech- on steels used in marine applications).[6] While the syntheses
nologies, the known biominerals (only about 60 different of calcium molybdate-based powdershas been accomplished
mineralshavebeenidentifiedtodate)donotpossesscompo- by methods based on solid-state reaction, coprecipitation,
sitionsthatareparticularlyattractiveformanyman-madede- combustionsynthesis,orpyrolysisoforganicprecursors,such
vices.[2] Nonetheless, nature’s exquisite control over biomin- powder processing has involved high-temperature firing for
eral formation has inspired the search for biomolecules extendedtimes(e.g.,500–1000°Cfor2–8h).[7]Newchemical
capable of directing the assembly of non-natural inorganic approachesthatallowfortherapidroom-temperaturesynthe-
materials.Peptidesthatexhibitspecificaffinitiesforsynthetic sis of calcium molybdate, as well as other functional multi-
materials (e.g., ZnO, Cr O , GeO , Ag, GaAs) have been component transition-metal oxide compounds, would enable
2 3 2
identified by several authors through bacteriophage or cell such compounds to be directly formed on low-temperature
surface display (biopanning)methods.[3] However,the use of substrates (e.g., flexible plastics and cloths) or concurrently
suchdisplaymethodstoidentifyspecificpeptidesthatinduce with low-temperature materials (e.g., coprecipitation with
the formation of crystalline multicomponent metal oxide low-melting organic or inorganic salts). Furthermore, the
compounds(i.e., materials widely used in functional devices) identificationofpeptidesthatlocallyinducetheprecipitation
at room temperature and ambient pressure has not been ofsuchmulticomponentoxidecompoundscouldallowforor-
reportedintheliterature.Inthiswork,aphagedisplaymeth- ganizedfunctionalstructuresatroomtemperature,thatis,the
od has been used to identify peptides that bind to, and pro- patterning of such peptides onto surfaces, followed by pep-
mote the direct and rapid room-temperature formation of tide-inducedmineralization,wouldyieldfunctionalmulticom-
CaO·MoO (powellite) microparticles from aqueous precur- ponentoxideswithtailoredmorphologies.
3
sor solutions. Microscale calcium molybdate-based powders ThesearchforCaMoO -formingpeptidesinvolvedtheuse
4
areattractiveasphosphorparticlesforadvancedlightingand of a commercially available phage display peptide library to
display applications (e.g., as stable and efficient red-light- identifypeptidesthatexhibitstrongbindingtoCaMoO pow-
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der.Afterfiveroundsofselectivepanning,fouruniquephage
clones with an affinity for calcium molybdate were isolated.
– The amino-acid sequences of the four displayed peptides
(labeledCM1toCM4),arelistedinTable1.
[*] Prof.K.H.Sandhage,Dr.G.Ahmad,M.B.Dickerson,
Precipitationassayswereconductedtoassesswhetherthese
Dr.B.C.Church,Dr.Y.Cai,Dr.J.S.King,Prof.C.J.Summers
SchoolofMaterialsScienceandEngineering peptides would promote the formation of CaMoO4 from
GeorgiaInstituteofTechnology aqueousprecursorsolutions.A25 lLquantityofa2 mgmL–1
771FerstDrive,Atlanta,GA30332-0245(USA)
solution of a given peptide in water was introduced into an
E-mail:[email protected]
S.E.Jones,Dr.R.R.Naik aqueoussolution of 0.5M calcium acetate and 0.2M ammoni-
AirForceResearchLaboratory,AFRL/MLPJ um paramolybdate at pH7 and room temperature. For each
3005HobsonWay,Bldg651 ofthefourCMpeptides,precipitationoccurredwithin20min
Wright-PattersonAFB,OH45433-7702(USA)
ofexposuretotheotherwisestablecalciumacetate–ammoni-
Dr.N.Kröger
um paramolybdate precursor solution. To confirm that such
SchoolofChemistryandBiochemistry
GeorgiaInstituteofTechnology precipitation resulted specifically from the presence of the
770StateStreet,Atlanta,GA30332–0400(USA) biopanned peptides, the following control experiments were
[**] ThisresearchwassupportedbytheAirForceOfficeofScientificRe- conducted.InsteadoftheCMpeptidesolutions,25 lLquanti-
search (Dr.J. Fuller, Dr.H.C. DeLong, program managers) and
tiesofeither:i)water,orii)a2 mgmL–1solutionofacontrol
theOfficeofNavalResearch(Dr.M.Spector).Supportinginforma-
tionisavailableonlinefromWileyInterScienceorfromtheauthors. peptide, CON1 or CON2 (see Table 1), were added to the
Adv.Mater.2006,18,1759–1763 ©2006WILEY-VCHVerlagGmbH&Co.KGaA,Weinheim 1759
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4. TITLE AND SUBTITLE 5a. CONTRACT NUMBER
Rapid, Room-Temperature Formation of Crystalline Calcium Molybdate
5b. GRANT NUMBER
Phosphor Microparticles via Peptide-Induced Precipitation
5c. PROGRAM ELEMENT NUMBER
6. AUTHOR(S) 5d. PROJECT NUMBER
5e. TASK NUMBER
5f. WORK UNIT NUMBER
7. PERFORMING ORGANIZATION NAME(S) AND ADDRESS(ES) 8. PERFORMING ORGANIZATION
Georgia Institute of Technology,School of Materials Science and REPORT NUMBER
Engineering,Atlanta,GA,30332-0245
9. SPONSORING/MONITORING AGENCY NAME(S) AND ADDRESS(ES) 10. SPONSOR/MONITOR’S ACRONYM(S)
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Prescribed by ANSI Std Z39-18
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A Table1. Amino-acid sequences and isoelectric point (pI) values of cal-
C ciummolybdate-bindingpeptides.
I
N
U Clonenumber Aminoacidsequence pI[a]
M CM1 AAPNSPWYAYEY 4.00
M CM2 SWSPAFFMQNMP 5.24
O CM3 YESIRIGVAPSQ 6.00
C CM4 DSYSLKSQLPRQ 8.59
CM3m1 YEAIRIGVAPSQ 6.00
CM3m2 YEAIRIGVAPAQ 6.00
CM3m3 YIVEIASGRPQS 6.00
CM3m4 YESIRISQLPRQ 8.75
CM4m DSYSKSRLQLPQ 8.59 c)
CON1 VLPPAIADAPLG 3.80 Mo
CON2 VVPLGMELRPRP 9.57
[a]CalculatedusingpI/massprogramatwww.expasy.ch
Relative
Intensity Au Ca
precursor solution. The control peptides did not exhibit spe-
cific binding to calcium molybdate and possessed isoelectric
point (pI) values that spanned the range of pI values of the
CMpeptides.Precipitationwasnotobservedforanyofthese
Ca
controlexperimentsorfortheprecursorsolutionalone,even
after6 hofincubation.
1.0 3.0 5.0 7.0
Scanningelectronmicroscopy(SEM)revealedthatthepre-
Energy (keV)
cipitates formedunderthe influence ofthe CaMoO binding
4
peptideswereaggregatesoffinerparticles.Asecondaryelec-
tron image of the aggregates formed in the presence of the d)
CM4peptideisshowninFigure1a.Theaggregateswerecom-
CaMoOO
prised of fine, roughly spherical particles that were a few 4
micrometersindiameter.Similaraggregatesofsphericalpar-
ticlesformedinthepresenceoftheotherthreeCMpeptides. Relative
The CM3 peptide also induced the formation of aggregates Intensity
comprised of larger, faceted particles (Fig.1b). Energy-dis-
persive X-ray (EDX) analyses of the spherical precipitates
formed in the presence of the four CM peptides, and of the
faceted precipitates formedin the presenceof the CM3 pep-
tide,indicatedthepresenceofbothcalciumandmolybdenum,
asshowninFigure1c(note:thegoldpeakintheEDXpattern 2θ (degrees)
wasduetoathingoldcoatingappliedtotheparticlestoavoid
charging in the electron microscope). X-ray diffraction Figure1.a,b)Secondaryelectronimagesoftheprecipitatesgeneratedat
(XRD) analysis of the precipitate induced by the CM3 pep- roomtemperatureinthepresenceoftheCM4andCM3peptides,respec-
tively. c,d)Energy dispersive X-ray analysis and X-ray diffraction (XRD)
tide is shown in Figure1d. Diffraction peaks for only Ca-
analyses,respectively,oftheprecipitategeneratedinthepresenceofthe
MoO (powellite)weredetected,thatis,peaksfortheoxides
4 CM3peptideatroomtemperature.
of calcium or molybdenum, or for other calcium molybdate
compounds(Ca MoO , CaMo O , Ca Mo O [8]) were
3 6 3.2 5.3 1.24 1.01 3
not observed. Electron diffraction analyses of particle cross Asmentionedabove,precipitationdidnotoccurinthepre-
sections also confirmed the presence of only CaMoO4 (data cursorsolution(0.5Mcalciumacetate,0.2Mammoniumpara-
not shown). Similar XRD patterns were obtained from the molybdate)fortimesaslongas6 hintheabsenceoftheCM
precipitates induced by the other CM peptides(see the Sup- peptides. In order to evaluate whether pure CaMoO would
4
porting Information).Hence, even though the molar ratio of precipitate from a more concentrated precursor solution, a
CatoMo(1:2.8)inthestartingprecursorsolutionwasmolyb- 2M aqueous solution of calcium acetate was mixed with an
denum-richrelativetothestoichiometryofCaMoO4,theCM equal amount of an aqueous 0.8M solution of ammonium
peptides induced the formation of only the latter compound paramolybdate (i.e., the precursor concentrations were
(i.e., the compound against which these peptides were se- doubled, while keeping the calcium acetate to ammonium
lectedbybiopanning).Thisfurtherindicatesthespecificityof paramolybdateratiofixed).Precipitationwasobservedtooc-
thesepeptidesforinducingpowelliteformation. curimmediatelyuponmixing.After2 h,thesupernatantwas
1760 www.advmat.de ©2006WILEY-VCHVerlagGmbH&Co.KGaA,Weinheim Adv.Mater.2006,18,1759–1763
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removedfromtheprecipitate,whichwasthendriedbyusing aa)) U
vacuumcentrifugation.Uponwashingoftheprecipitatewith N
deionized(DI)wateritwasobservedthatmostoftheprecipi- I
C
tatewaslostthroughdissolution.Inasubsequentexperiment A
undersimilarprecipitationconditions,theprecipitatewasnot T
I
washedafterremovalofthesupernatantandvacuumcentrifu- RReellaattiivvee O
N
gation. XRD analysis revealed the presence of substantial WWeeiigghhtt %%
S
amounts of ammonium molybdenum oxide hydrate
([NH ] Mo O ·4H O)andlime(CaO)alongwithpowellite
46 8 27 2
in the precipitate (shown in Fig.2S of the Supporting Infor-
mation). For comparison, the precipitate formed after only
10minofincubationoftheoriginal precursorsolution(0.5M
calcium acetate, 0.2M ammonium paramolybdate) with the
CM3 peptide was also examined by XRD analysis without
TTeemmppeerraattuurree ((ººCC))
washingthe precipitatewith DIwater.The XRD patternfor
thisprecipitate (shownin Fig.2S of the SupportingInforma- bb)) 3300
tion)yieldeddiffractionpeaksforonlyCaMoO (i.e.,thedif-
4
fractionpatternwassimilartothatshowninFig.1d).Hence,
while a solid mixture containing some CaMoO could be 2255
4
formedfromasupersaturatedprecursorsolution,onlytheuse
of the CM-binding peptides allowed for the rapid formation
2200
ofpureCaMoO fromasolubleprecursorsolution.
4
The photoluminescence emission of peptide-induced cal- CM//PPep
ciummolybdateparticleswasevaluatedusing300nmUVex- Rattiioo
1155
citationatroomtemperature.Arepresentativephotolumines- (mgg//mg)
cence spectrum obtained from the precipitate formed in the
presence of the CM3 peptide is shownin Figure2. An emis- 1100
sion peak centered around 530nm (green) was observed,
whichissimilartothatreportedpreviouslyforCaMoO .[4a,7c]
4
ToquantifytheamountofCaMoO formedinthepresence 55
4
ofagivenCMpeptide,theprecipitatedmaterialwasdriedfor
16h at 65°C, and then subjectedto thermogravimetric (TG)
00
analyseswhileheatingat5°Cmin–1upto600°Cinair.Arep-
CCMM11 CCMM33 CCMM33mm22 CCMM33mm44 CCMM44mm CCOONN22
resentative TG analysis of the precipitate generated in the
CCMM22 CCMM33mm11 CCMM33mm33 CCMM44 CCOONN11
presence of the CM3 peptide is shown in Figure3a. The
Peptide
weight loss due to evaporation and pyrolysis was completed
uponheatingtoabout400°C.Thetotalweightlossafterheat-
Figure3.a)TGanalysisrevealingtheweightlossofthedriedCaMoO
4
ingto600°Cwasonly13.5%,whichindicatedthattheprecip- precipitategeneratedfromtheCM3peptideuponheatingat5°Cmin–1
itatewascomprisedof86.5wt%CaMoO4.Quantitativeanal- to600°Cinair.b)TheratiooftheweightofCaMoO4precipitategener-
ated per weight of peptide (CM/Pep ratio) for the peptides listed in
Table1(forsimilarexposuretimesof2h).
ysesoftheamountofCaMoO formeduponexposurefor2 h
4
to each of the CM peptides is indicated in Figure3b. These
datawereobtainedby measuringtheweight ofeach precipi-
Relative
tateafterheatingat5°Cmin–1to600°Cinair(i.e.,aftercom-
Intensity
pleteevaporationofthevolatileconstituentsandpyrolysisof
the organic material presentwith the precipitated CaMoO ).
4
While all the peptides, CM1–CM4, induced the formation of
significant amounts of calcium molybdate (i.e., >6mg Ca-
MoO per mg of peptide), the CM3 peptide generated the
4
largest amount of CaMoO (27mg CaMoO per mg of pep-
4 4
Wavelength (nm) tide).
Although all four CM peptides exhibited selective binding
Figure2.Photoluminescencespectrum,obtaineduponstimulationwith
affinities for CaMoO , and induced the rapid formation of
300nmlight,oftheCaMoO4precipitategeneratedinthepresenceofthe 4
CM3peptide. only this compound from the precursor solution, the amino-
Adv.Mater.2006,18,1759–1763 ©2006WILEY-VCHVerlagGmbH&Co.KGaA,Weinheim www.advmat.de 1761
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A acid sequences of these four peptides were surprisingly di- ThepowderwasplacedintheTBSTsolution(5mgCaMoO to1mL
4
C verse(seeTable 1).Noapparenthydrophobic,hydrophilic,or TBST)andthenexposedtothephagesolution(10lLofphagesolu-
NI charged sequences were conserved among all four peptides. tionper5mgofCaMoO4)foratotaltimeof1hatroomtemperature
U on a rotator operating at 25rpm. After such exposure, the powder
However,allfourCMpeptidespossessedatleasttwohydrox- wasvigorouslywashedtentimeswith1mLofaTBSTsolution,con-
M
yl-bearingaminoacids(serine,threonine,tyrosine).Itisinter- taining 0.5% Tween-20at pH7.5 with tris-hydroximethyaminoethy-
M estingtonotethatspecificserineresidueshavebeenfoundto lene,toremoveanyunboundorlooselyboundphageparticles.The
O becritical forthecomplexationofmolybdenumintheactive powder was then exposed to a solution of 0.2M glycine with HCl
C sites of certain bacterial enzymes.[9a,b] Furthermore, three of (pH2.20)for7mintoelutethephageparticlesadheringtotheCa-
MoO.TheelutedphageparticlesweretransferredtoanewEppen-
4
theCMpeptides(CM1,CM3,CM4)containedaresiduewith dorftubeandneutralized(topH7.0)withtheadditionof150lLof
a second negatively charged carboxylate group (aspartate, theTBSTsolution.Theelutedphageparticleswereamplifiedbyincu-
bation for 4.5h with Escherichia coli K12 host cells that had been
glutamate) in addition to the C-terminal carboxylate group.
grownovernightonLuriaBroth(LB)medium.Thebiopanningpro-
Li et al. have previously reported that calcite-binding pep-
cess(exposuretoCaMoO powder,washing,acidelution,amplifica-
4
tides, identified from a phage display library, exhibited an tion)wasrepeatedfourtimestofurtherisolateandenrichthecalcium
enrichment in hydroxyl-bearing, or hydroxyl- and carboxyl- molybdate-bindingphage.Afterthefinalroundofpanning,Escheri-
ate-bearing,amino-acidresidues.[9c] chiacolihostcellswereinfectedwiththeelutedphageandspreadon
LB(FisherScientific,USA)platescontaining5-Bromo-4-Chloro-3-in-
MutationsoftheCM3andCM4peptideswereusedtoeval-
dolyl-b-D-galactopyranoside(X-gal,Invitrogen,Carlsbad,CA,USA)
uatetheinfluenceoftheserineresiduesonCaMoO4precipi- and isopropyl-b-D-thiogalactopyranoside (IPTG, Invitrogen). DNA
tation (see Table 1). When one or both serine residues were obtainedfrom the phage clones was sequencedusingan automated
replaced by alanine, the amount of CaMoO formed within sequencer(ABI310,PEAppliedBiosystems,FosterCity,CA).Pep-
4 tides weresynthesizedby a commercial vendor(New EnglandPep-
2 h was reduced by 32–38% (compare CM3m1 and CM3m2
tides,Gardner,MA,USA).
toCM3inFig.3b).Whentherelativepositionsoftheamino For precipitation assays, precursor solutions of calcium acetate
acidswerealtered,withoutchangingtheamino-acidcomposi- (Ca(CHO) ·HO,99%purity,AlfaAesar)andammoniumpara-
2 5 2 2 2
tions, the CaMoO4 yield was again significantly reduced molybdate ((NH4)6Mo7O24·4H2O, 99% purity, Alfa Aesar) were
preparedinDIwater(Nano-PureDiamondUltrapureWaterSystem,
(CM3m3generated32%lessCaMoO thanCM3,andCM4m
4 BarnsteadInternational,Dubuque,IAUSA).A100lLquantityofa
generated69%lessCaMoO4thanCM4).Replacementofthe 1Mcalciumacetateaqueoussolutionwasmixedwith100lLofa0.4M
last six residues at the C terminus of the CM3 peptide with solutionofammoniumparamolybdateatpH7.Agivenprecipitation
thelastsixC-terminalresiduesoftheCM4peptideresultedin assaywasinitiatedbyintroducing25lLofaparticularpeptidesolu-
tion(2mgmL–1)tothisprecursorsolutionatroomtemperature.The
a62%reductionintheamountofcalciummolybdateformed
concentrations of individual peptides in solution were evaluated by
(compare CM3m4 to CM3 in Fig.3b). However,the amount spectrophotometricanalysisat280nm,usingtheknownmolarextinc-
of CaMoO formed with the CM3m4 peptide was similar to tioncoefficientsoftryptophanandtyrosine.Theprecipitatesformed
4
thatfortheCM4peptide(note:thepIoftheCM3m4mutant after2hinthepresenceofthepeptideswerewashedthreetimeswith
DIwaterandthenwithmethanol.Theprecipitates werethendried
wasclosetothatoftheCM4peptide).Theseresultsindicate
for16hat65°C.
that the serine content, the positions of the amino-acid resi-
SEM was conducted using a field emission gun microscope
dues,andtheacidity/basicityofthescreenedCMpeptidesin- (Leo1530 FEG SEM, Carl Zeiss SMT Ltd., Cambridge, UK)
fluencetheamountofCaMoO formedatroomtemperature. equipped with an EDX spectrometer (INCA EDS, Oxford Instru-
4
ments,Bucks,UK).Transmissionelectronmicroscopywasconducted
To the authors’ knowledge, this work is the first report of
withaJEOL4000EXinstrument.XRDanalyses(PhilipsPW1800,
theuseofphage-display-screenedpeptidestoinducetherap-
PANalytical Almelo, The Netherlands) were conducted with CuKa
id, room-temperatureformationofa specific functionalcrys- radiation at a scan rate of 0.6°min–1. TG analyses were conducted
talline multicomponent oxide compound (CaO·MoO ). The with a Netzsch449C Simultaneous Thermal Analyzer (Selb, Ger-
3
many).QuantitativeanalysesoftheamountofCaMoO formedupon
directformationofsuchbinaryoxidecompoundswithoutthe 4
exposuretoeachoftheCMpeptideswereobtainedbymeasuringthe
needforfiringatelevatedtemperaturesopensthedoortothe weightofeachprecipitateafterheatingat5°Cmin–1to600°Cinair.
biosculpting (peptide patterning, then localized peptide-in- The photoluminescence emission spectrum of peptide-induced cal-
duced mineralization) of functional compounds onto or with cium molybdate particleswasevaluatedat roomtemperature, using
low-temperatureorchemicallydissimilarmaterials. chopped(100Hz,ChopperSyncII,Spiricon,Logan,UT)300nmUV
excitationfroma300wattXenonarclamp(OrielInstruments,Strat-
ford,CT)coupledtoa1/4metermonochromater(Cornerstone260,
Oriel Instruments).Thepowderspecimens wereexcitedat 45° inci-
Experimental dence, andtheresultingemissionwascollected at normalincidence
usingacollimatinglens(74-UV,OceanOptics,Dunedin,FL)andafi-
berprobe(LG-455-020-3,ActonResearchCorp.,Acton,MA).Thefi-
Acommercialcombinatorialphagedisplaypeptidelibrary(PhD12 ber probe was coupled to an emission monochromator (Spectra
kit, New England Biolabs, Beverly, MA, USA) was used to isolate Pro500i, Acton Research Corp.), affixed with a thermoelectrically
peptidesthatbindtocalciummolybdate(CaMoO4)powder(99.9% cooled photosensor module (H7422-50, Hamamatsu Corp., Bridge-
purity,AlfaAesar,WardHill,MAUSA).Priortothebiopanningex- water,NJ).Thedetectedsignalwasacquiredusingalock-inamplifier
periments,thepowderwasvigorouslywashed(byvortexingandcen- (SignalRecovery5210,OakRidge,TN).
trifugation) ten times with 1mL of a tris-buffered saline Tween
(TBST)solutioncomprising0.2%Tween-20bufferedatpH7.5with Received:February7,2006
tris-hydroximethyaminoethylene (AMRESCO, Solon, OH, USA). Finalversion:April26,2006
1762 www.advmat.de ©2006WILEY-VCHVerlagGmbH&Co.KGaA,Weinheim Adv.Mater.2006,18,1759–1763
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