Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
Permanent URI for this collectionhttps://hdl.handle.net/11147/7148
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Article Citation - WoS: 5Citation - Scopus: 5Novel Biopolymer-Based Hydrogels Obtained Through Crosslinking of Keratose Proteins Using Tetrakis(hydroxymethyl) Phosphonium Chloride(Springer, 2022) Yalçın, Damla; Top, AybenMerino wool obtained from the Karacabey region of Turkey was solubilized using peracetic acid oxidation. The wool and extracted wool proteins (keratose) were characterized using SEM, XRD, TGA, and FTIR analyses. SDS-PAGE result of the keratose indicated diffusive bands were populated between ~ 40 and ~ 55 kDa, corresponding to low-sulfur content α-keratose proteins. Chemically crosslinked hydrogels were prepared using the keratose and tetrakis(hydroxymethyl) phosphonium chloride (THPC). Storage moduli of the hydrogels prepared at 1:1, 1:2, and 1:4 keratose to THPC reactive group ratios were measured as 63 ± 22, 291 ± 21, and 804 ± 53 Pa, respectively. Crosslinking degrees of the hydrogels also affected the secondary structures of the keratose films obtained from the drying of the hydrogels. The hydrogel with the highest crosslinking density (1:4 gel) exhibited the lowest swelling ratio, whereas the one with the lowest crosslinking density (1:1 gel) disintegrated in deionized water within less than 6 h. CCK-8 tests using L929 mouse fibroblast cells showed that all the hydrogels promoted cell proliferation. These results suggest THPC crosslinked hydrogels prepared at the millimolar THPC concentrations are biocompatible scaffolds, which can be utilized in drug delivery and tissue engineering applications. Graphical abstract: [Figure not available: see fulltext.]Article Citation - WoS: 4Citation - Scopus: 4Optical and Photocatalytic Properties of Zno and Zns Structures Formed as Controlled Calcination Products of L-Cysteine Assisted Aqueous Precipitation(Elsevier, 2020) Şen, Selin; Top, AybenZnO and ZnS structures were obtained by the calcination of the aqueous precipitation products of Zn(NO3)2, NaOH and L-cysteine (Cys). Initial Cys:Zn molar ratios were changed as 0.1:1, 0.5:1, 1:1 and 1.5:1. All the precursors were transformed into ZnO upon calcination at 700 °C. ZnS structures were obtained by calcining the precursors prepared at the Cys:Zn ratios of 1 and 1.5 at 350 °C. In addition to changing chemical composition of the precipitation products, calcination temperature and initial Cys:Zn ratio also affected morphology, surface area, photoluminescence and photocatalytic properties of the final products. Free exciton energy values of the ZnO samples were observed to be between 3.29 eV and 3.35 eV. PL spectra of the ZnO samples indicated blue and green emission centers. Zinc interstitials (Zni), revealed by the blue emissions in the PL spectra were also confirmed by Auger Zn L3M4.5M4.5 spectra. The samples calcined at 350 °C removed rhodamine B mainly by adsorption. All the samples calcined at 700 °C successfully degraded the dye under UV light. Among the samples calcined at 700 °C, ZnO sample prepared at Cys:Zn = 0.5, which has the highest surface area and unique photoluminescence spectrum exhibited the fastest photodegradation rate. © 2020 Elsevier LtdArticle Citation - WoS: 12Citation - Scopus: 12Peg and Peg-Peptide Based Doxorubicin Delivery Systems Containing Hydrazone Bond(Springer Verlag, 2018) Balcı, Beste; Top, AybenmPEG and mPEG-peptide based drug delivery systems were prepared by conjugating doxorubicin (DOX) to these carrier molecules via hydrazone bond. The peptide, AT1, with a sequence of CG3H6G3E served as mPEG and doxorubicin attachment site. Histidines were incorporated to the sequence to improve pH responsiveness of the carrier molecule. Hydrodynamic diameters (mean sizes) of mPEG-based drug delivery system (mPEG-HYD-DOX) were measured as 9 ± 0.5 and 7 ± 0.5 nm at pH 7.4 and pH 5.0, respectively. Mean size of the aggregates of the peptide containing drug delivery system, mPEG-AT1-DOX, was determined as 12 ± 2 nm at neutral pH. At pH 5.0, on the other hand, mPEG-AT1-DOX exhibited a size distribution between 20 and 100 nm centered at about 40 nm. Comparison of % DOX release values of the drug delivery systems obtained at pH 7.4 and pH 5.0 indicated that mPEG-AT1-DOX has enhanced pH sensitivity. DOX equivalent absolute IC50 values were obtained as 0.96 ± 0.51, 21.9 ± 5.9, and 5.55 ± 0.75 μg/mL for free DOX, mPEG-HYD-DOX, and mPEG-AT1-DOX, respectively. Considering more pronounced pH sensitivity and cytotoxicity of mPEG-AT1-DOX, the use of both pH responsive functional groups and acid cleavable chemical bond between the carrier molecule and drug can be a promising approach in the design of drug delivery systems for cancer therapy.Article Citation - WoS: 25Citation - Scopus: 25Conformational and Aggregation Properties of a Pegylated Alanine-Rich Polypeptide(American Chemical Society, 2011) Top, Ayben; Roberts, Christopher J.; Kiick, Kristi L.The conformational and aggregation behavior of PEG conjugates of an alanine-rich polypeptide (PEG-c17H6) were investigated and compared to that of the polypeptide equipped with a deca-histidine tag (17H6). These polypeptides serve as simple and stimuli-responsive models for the aggregation behavior of helix-rich proteins, as our previous studies have shown that the helical 17H6 self-associates at acidic pH and converts to β-sheet structures at elevated temperature under acidic conditions. In the work here, we show that PEG-c17H6 also adopts a helical structure at ambient/subambient temperatures, at both neutral and acidic pH. The thermal denaturation behavior of 17H6 and PEG-c17H6 is similar at neutral pH, where the alanine-rich domain has no self-association tendency. At acidic pH and elevated temperature, however, PEGylation slows β-sheet formation of c17H6, and reduces the apparent cooperativity of thermally induced unfolding. Transmission electron microscopy of PEG-c17H6 conjugates incubated at elevated temperatures showed fibrils with widths of ∼20-30 nm, wider than those observed for fibrils of 17H6. These results suggest that PEGylation reduces β-sheet aggregation in these polypeptides by interfering, only after unfolding of the native helical structure, with interprotein conformational changes needed to form β-sheet aggregates.Article Citation - WoS: 12Citation - Scopus: 12Controlling Assembly of Helical Polypeptides Via Pegylation Strategies(Royal Society of Chemistry, 2011) Top, Ayben; Zhong, Sheng; Yan, Congqi; Roberts, Christopher J.; Pochan, Darrin J.; Kiick, Kristi L.Recent studies in our laboratories have demonstrated that a helical polypeptide (17H6), equipped with a histidine tag and a helical alanine-rich, glutamic-acid-containing domain, exhibits pH-responsive assembly behavior useful in the production of polymorphological nanostructures. In this study, the histidine tag in these polypeptides was replaced by polyethylene glycol (PEG) with different molecular masses (5 kDa, or 10 kDa), and the self-association behavior of 17H6 and the PEGylated conjugates was characterized via dynamic light scattering (DLS), small angle neutron scattering (SANS), and cryogenic transmission electron microscopy (cryo-TEM). DLS experiments illustrated that the polypeptide and its PEG-conjugates undergo reversible assembly under acidic conditions, suggesting that the aggregation state of the polypeptide and the conjugates is controlled by the charged state of the glutamic acid residues. Nanoscale aggregates were detected at polypeptide/conjugate concentrations as low as 20 μM (∼0.3-0.5 mg ml -1) at physiological and ambient temperatures. Scattering and microscopy results showed that the size, the aggregation number, and the morphology of the aggregates can be tuned by the size and the nature of the hydrophilic tag. This tunable nature of the morphology of the aggregates, along with their low critical aggregation concentration, suggests that PEG-alanine-rich polypeptide conjugates may be useful as drug delivery vehicles in which the alanine-rich block serves as a drug attachment domain.