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Faj gösterim ile platin yüzeylere spesifik peptidlerin seçimi/karakterizasyonu/sentezi ve bunların ışığa duyarlı nano-hibridlerinin hazırlanması Skip to content Tez Künye Durumu Faj gösterim ile platin yüzeylere spesifik peptidlerin seçimi/karakterizasyonu/sentezi ve bunların ışığa duyarlı nano-hibridlerinin hazırlanması / Selection/characterization/synthesis of peptides specific to platinum surfaces by phage display and preparation of their light sensitive nano-hybrid forms Yazar:SEVİL DİNÇER Danışman: PROF.DR. ERHAN BİŞKİN ; PROF.DR. MEHMET SARIKAYA Yer Bilgisi: Hacettepe Üniversitesi / Fen Bilimleri Enstitüsü / Biyomühendislik Ana Bilim Dalı Konu:Biyoloji = Biology ; Biyomühendislik = Bioengineering ; Kimya = Chemistry Dizin: Onaylandı Doktora Türkçe 2006 160 s. Bu çalışmada amaç, M13 faj gösterim kütüphanesi kullanılarak platin metalinespesifik peptidlerin seçilmesi, bu peptidlerden birini kullanarak, ışığa duyarlı molekülile bağlanarak oluşturulan hibrid moleküllerin platin yüzey üzerine bağlanmakarakteristiklerinin incelenmesidir.Çalışmanın ilk kısmında faj gösterim tekniği uygulanmıştır. Bu amaçla, uygunyöntemlerle temizlenen platin metali faj kütüphanesi ile etkileştirilmiş, bağlanan fajlarayrılmış, E.coli’ye infeksiyon ile çoğaltılıp, PEG/NaCl ile çöktürülerek saflaştırılmış veDNA izolasyonu yapılarak peptid dizileri ortaya çıkartılmıştır. Toplam 34 adet peptiddizisi elde edilmiş, bu peptidler çeşitli özelliklerine göre incelenmiştir. İstatistikselanaliz sonucunda glutamin (Q), asparjin (N), serin (S), treonin (T), glisin (G), valin(V), lisin (K) ve glutamik asit (D) aminoasitlerinin diğerlerine göre daha fazlagözlendiği tespit edilmiştir. Ayrıca, ClustalW ile yapılan dizi analizi sonucunda, T/S-X-T/S üçlüsünü içeren aminoasitlere sıklıkla rastlandığı görülmüş, bu üçlüyü içerenpeptidlerde, polar ve bazik aminoasitlerin sıklıkla rastlandığı, bunların yüksüz ya dapozitif yüklü olduğu, bağlanmada bu motifin rol oynayabileceği sonucuna varılmıştır.Bu üçlüyü içermeyen peptidlerde ise özellikle hidroksil grubu taşıyan aminoasitlererastlanmadığı görülmüş, böylece, tiyol grubu ile metallere bağlanma konusundahidroksil gruplarına bağlı bir alternatifin olabileceği sonucuna varılmıştır. Yapılan FManalizlerinde ise, T/S-X-T/S üçlüsünü içeren peptidleri taşıyan bakteriyofajların,platine daha yüksek sepsifitede bağlandığı, diğerlerinin az bağlanma gösterdiği tespitedilmiştir. Ayrıca, kontrol olarak kullanılan ZnS’e zayıf bağlanma gözlenmiştir. FManalizinde iyi sonuç veren SD152 kodlu peptidi taşıyan fajın cam üzerinemakrodesen şeklinde hazırlanmış platin malzemeyi tanımasına ilişkin FMçalışmasına göre, platine bağlanmanın çok spesifik olduğu, cam üzerine bağlanmaolmamasından anlaşılmıştır. Modelleme çalışması ile, platin yüzeyi tanıyanpeptidlerde yüzey ile yakın temas halinde bulunan grupların yüksek oranda hidroksilgrupları olduğu gösterilmiş, bağlanmada bu grupların rol oynayabileceği yargısıdoğrulanmıştır.Çalışmanın diğer bölümünde, buraya kadar yapılan analizler sonucunda platin yüzeyitanımada en yüksek spesifiteyi gösteren peptidlerden biri olan SD152 kimyasalolarak sentezlettirilerek devam edilmiştir. Öncelikle ışık duyarlı 4-hidroksiazobenzen-4-sülfonik asit molekülü sentezlenmiş ve yapısal analiz FTIR, NMR ilegerçekleştirilirken, UV-spektrofotometre ile ışık duyarlılık gösterilmiştir. Ardından,azobenzen ile peptid (SD152) kimyasal olarak CDI aktivasyonu ile bağlanmış,aktivasyonun başarılı olduğu FTIR analizi ile, bağlanmanın gerçekleştiği ise 1H-NMRile gösterilmiştir. Peptid bağlanma verimi ninhidrin yöntemi ile %60 olarakbelirlenmiştir. Peptid bağlı azobenzenin ışığa duyarlılığını koruduğu gözlenmiş vereaksiyon hız sabiti 1.1.10-3 dak -1 olarak hesaplanmıştır. Peptid bağlı azobenzeninabsorbans davranışı değişik pH’larda incelenmiş ve çok bazik pH’larda azobenzeneait geçiş piklerini kaydırdığı görülmüştür. Peptid bağlı azobenzenin organik ortamdada izomerizasyon gösterebildiği fakat absorbsiyon maksimumlarının farklıdalgaboylarına kaydığı gözlenmiştir. QCM deneyleri ile peptid ve azobenzen bağlıpeptidin yüzeye bağlanma karakteristikleri incelenmiştir. Peptidin platin yüzeyemaksimum bağlanma gösterdiği derişim 5.76.10-7M, pH ise 7.4 olarak bulunmuştur.Yüzeydeki peptid absorbsiyonunun zamana bağımlı değişiminin Langmuirizomtermine uyarlanması sonucunda, peptidin platin yüzey üzerinde düzgün tektabaka oluşturduğu, Langmuir kinetiğine uyduğu belirlenmiştir. SYSTAT 10 ile yapılankinetik çalışma sonucunda, peptidin platin yüzeye bağlanma sabitleri, kb=2.9.104,ka=0.0167, Kd=1.8.106 M -1 olarak bulunmuş, âGads değeri ise -8.5 kcal/mol olarakhesaplanmış, peptidin Pt üzerine kendiliğinden, düzgün yerleştiği sonucunavarılmıştır. Azobenzen bağlı peptid için ise, kb=7.8.104, ka =0.0165, Kd= 4.7.106 M-1,âGads= -9.1 kcal/mol olarak hesaplanmış, azobenzen molekülünün peptidebağlanmasının platin yüzeyi tanımasına engel olmadığı görülmüştür. Peptid ileazobenzen bağlı peptidin platin yüzeye yerleştirildikten sonra yapılan temas açısıölçümleri sonucunda ise, hidrofilik yüzeyler elde edilmiştir.Sonuç olarak, ışığa duyarlı nanohibrid yapıların platin yüzeyi kendiliğinden birarayagelme yoluyla spesifik olarak tanıdığı görülmüştür. Bu çalışma ile, akıllı sistemleringeliştirilmesine olanak sağlayabilecek kontrollü olarak özellikleri değişitirilebilenyüzeyler elde edilmiştir.Anahtar Kelimeler: Faj gösterim, platin, kendiliğinden biraraya gelme, biyobenzetim,azobenzen, ışık duyarlı molekül, CDI aktivasyonu, QCM, akıllı yüzeylerTez Danışmanı: Prof. Dr. Erhan Bişkin, Hacettepe Üniversitesi Kimya MühendisliğiBölümüOrtak Danışman: Prof. Dr. Mehmet Sarıkaya, Washington Üniversitesi, MalzemeBilimi ve Mühendisliği Bölümü In this study, platinum-spesific peptides were selected by using M13 phage displaylibrary and binding characteristics of nanohybrid structures consisting one of theselected peptides coupled to a light-sensitive molecule on platinum surfaces wereinvestigated.First, peptide selection was performed. Cleaned platinum metal was interacted withphage library and unbound phage was eliminated. Bound phage was eluted from theplatinum surface and amplified by infection to E.coli. Then, phage was purified byPEG/NaCl precipitation. Purified phage DNA was isolated, labelled and amplified byPCR and sequenced. Totally 34 peptide sequence were obtained and they werecharacterized by different techniques. Statistical analyses showed that glutamine (Q),aspargine (N), serine (S), threonine (T), glycine (G), valine (V), lysine (K) andglutamic acid (D) were in higher abundance comparing to other amino acids.ClustalW sequence alignment revealed that some of peptides possess T/S-X-T/Striplet and these peptides have usually basic, positively charged/neutral and polarresidues. Peptides which do not possess this triplet did not have similarcharacteristics with the other peptides. The presence of mostly hydroxyl containingamino acid residues among the binders may be a result of a new binding mechanismthat is alternative to the well-known thiol-based systems. Two sets of cross-specificityexperiments were carried out. In the first, binding affinities were assessed using ZnSpowder, a semiconductor. While peptides carrying T/S-X-T/S triplet showed a goodbinding on platinum, the others did not. The second set was performed ascompetitive binding of a a selected binder possessing T/S-X-T/S triplet(SD152) on aPt macropatterned glass. The phage with a Pt binding peptide motif resulted in highspecificity to Pt regions as compared to the substrate matrix containing bare glass.Conformational analysis of a strong binder on three different platinumicrystallographic surfaces also indicates that threonine and serine as well asglutamine are in close and broad contact with the surfaces forming a tripod moleculararchitecture.Second, one of the good binders (SD152) was selected and chemically synthesizedand used for the next part of the studies. Light-sensitive 4-hydroxyazobenzene-4-sulfonic acid molecule was synthesized by azo-coupling reaction and characterizedby FTIR, NMR UV-spectrophotometer. Then, peptide (SD152) was coupled toazobenzene molecule by CDI activation. Activation and binding were demonstratedby FTIR and NMR, respectively. Efficiency of peptide incorporation was analyzed byninhydrin assay and found as 60%. It was observed that peptide-modifiedazobenzene had still light-sensitivity. Reaction rate constant was calculated as1.1.10-3 m i n -1 for trans-to-cis isomerization. It was also estimated that peptide-modified azobenzene showed different absorbance behaviour in basic pH. Peptide-modified azobenzen showed photoisomerization in organic medium (DMSO) but witha different absorption peak values. According to QCM experiments, maximumpeptide binding on platinum was observed at 5.76.10-7M concentration and pH: 7.4.Peptide adsorption was investigated depending on time in different concentrations.By fitting these experimental data to Langmuir isotherm with SYSTAT 10 modellingprogram, it was observed that peptide could self-assemble on platinum with highaffinity. Binding constants were calculated by ths kinetic study and found aska=2.9.104, k d=0.0167, Keq=1.8.106 M -1 olarak bulunmuş, âGads değeri ise -8.5kcal/mol. Similar experiments were also performed for azobenzene-coupled peptideand binding constants were calculated ka=7.8.104, k d=0.0165, K eq= 4.7.10 6 M -1,âGads= -9.1 kcal/mol. According to the kinetic study, azobenzene did not reveal anynegative effect on platinum binding. It was demonstrated that peptide andazobenzene-coupled peptide recognized platinum surface with a high binding affinity.Contact angle studies showed that peptide and azobenzene-coupled peptidescaused hydrophilicity on platinum surfaces.iiAs a result, it was observed that light-sensitive, nanohybrid structures recognizedplatinum by self-assembling. By this study, controlled-switchable surfaces which canbe employed for construction of smart devices was obtanied.Keywords: Phage display, platinum, self-assembling, biomimetics, azobenzene,light-sensitive molecule, CDI activation, QCM, smart surfacesAdvisor: Prof. Dr. Erhan Bişkin, Hacettepe Üniversity, Chemical EngineeringDepartment, Beytepe, Ankara.Co-advisor: Prof. Dr. Mehmet Sarıkaya, University of Washington, Material Scienceand Engineering Department, Seattle, WA, USA.iii
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