Researcher:
Kepsütlü, Burcu

Profile Picture
ORCID

Job Title

Master Student

First Name

Burcu

Last Name

Kepsütlü

Name

Name Variants

Kepsütlü, Burcu

Email Address

Birth Date

Filters

2012 - 20144

Advanced Search

Filter by

Settings

Researcher Of Publications: search.filters.isAuthorOfPublication.0bbffc30-bcdb-4776-9426-9fdad44d2a61

Search Results

Now showing 1 - 4 of 4
  • Placeholder
    PublicationMetadata only
    Characterization of protein release from poly(ethylene glycol) hydrogels with crosslink density gradients
    (Wiley, 2014) N/A; N/A; Department of Chemical and Biological Engineering; Bal, Tuğba; Kepsütlü, Burcu; Kızılel, Seda; PhD Student; Master Student; Faculty Member; Department of Chemical and Biological Engineering; Graduate School of Sciences and Engineering; Graduate School of Sciences and Engineering; College of Engineering; 353534; N/A; 28376
    Transplantation of cells within poly(ethylene glycol) (PEG) hydrogel scaffolds as effective immunoisolation barriers is becoming increasingly important strategy for tissue engineering and regenerative medicine. In these applications, crosslink density of these membranes has significant effect on the control of diffusion of many biomolecules such as nutrients, cellular wastes, and hormones. When these networks are designed with crosslink density gradients, alterations in network structure may have an effect on biomolecule diffusivity. The goal of this work was to synthesize PEG hydrogels via surface initiated photopolymerization for use in applications involving physiological protein delivery and cell encapsulation. For this purpose, PEG hydrogels of differing crosslink density gradients were formed via surface initiated photopolymerization, and the diffusion of model proteins with various molecular weights were observed through these PEG hydrogel scaffolds with defined properties. Diffusion coefficients were on the order of 10(-7)-10(-8) cm(2)/s and protein diffusion time scales varied from 5 min to 30 h. The results confirm that synthetic PEG hydrogels with crosslink density gradients are promising for controlled release of bioactive molecules and for covalent incorporation of ligands to support cell viability. (c) 2013 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 102A: 487-495, 2014.
  • Placeholder
    PublicationMetadata only
    Quantification of interactions among circadian clock proteins via surface plasmon resonance
    (Wiley, 2014) N/A; N/A; Department of Chemical and Biological Engineering; Department of Chemical and Biological Engineering; Kepsütlü, Burcu; Kızılel, Rıza; Kızılel, Seda; Master Student; Researcher; Faculty Member; Department of Chemical and Biological Engineering; Graduate School of Sciences and Engineering; College of Engineering; College of Engineering; N/A; 114475; 28376
    Circadian clock is an internal time keeping system recurring 24h daily rhythm in physiology and behavior of organisms. Circadian clock contains transcription and translation feedback loop involving CLOCK/NPaS2, BMaL1, Cry1/2, and Per1/2. in common, heterodimer of CLOCK/NPaS2 and BMaL1 binds to EBOX element in the promoter of Per and Cry genes in order to activate their transcription. CRY and PER making heterodimeric complexes enter the nucleus in order to inhibit their own BMaL1-CLOCK-activated transcription. the aim of this study was to investigate and quantify real-time binding affinities of clock proteins among each other on and off DNa modes using surface plasmon resonance. the pairwise interaction coefficients among clock proteins, As well as interaction of PER2, CRY2, and PER2:CRY2 proteins with BMaL1:CLOCK complex in the presence and absence of EBOX motif have been investigated via analysis of surface plasmon resonance data with pseudo first-order reaction kinetics approximation and via nonlinear regression curve fitting. the results indicated that CRY2 and PER2, BMaL1, and CLOCK proteins form complexes in vitro and that PER2, CRY2 and PER2:CRY2 complex have similar affinities toward BMaL1:CLOCK complex. CRY2 protein had the highest affinity toward EBOX complex, whereas PER2 and CRY2:PER2 complexes displayed low affinity toward EBOX complex. the quantification of the interaction between clock proteins is critical to understand the operation mechanism of the biological clock and to address the behavioral and physiological disorders, and it will be useful for the design of new drugs toward clock-related diseases.
  • Placeholder
    PublicationMetadata only
    Design of bioartificial pancreas with functional micro/nano-based encapsulation of islets
    (Bentham Science Publ Ltd, 2014) N/A; N/A; N/A; N/A; Department of Chemical and Biological Engineering; Kepsütlü, Burcu; Nazlı, Caner; Bal, Tuğba; Kızılel, Seda; Master Student; PhD Student; PhD Student; Faculty Member; Department of Chemical and Biological Engineering; Graduate School of Sciences and Engineering; Graduate School of Sciences and Engineering; Graduate School of Sciences and Engineering; College of Engineering; N/A; N/A; 353534; 28376
    Type I diabetes mellitus (TIDM), a devastating health issue in all over the world, has been treated by successful transplantation of insulin secreting pancreatic islets. However, serious limitations such as the requirement of immunosuppressive drugs for recipient patients, side effects as a result of long-term use of drugs, and reduced functionality of islets at the transplantation site remain. Bioartificial pancreas that includes islets encapsulated within semi-permeable membrane has been considered as a promising approach to address these requirements. Many studies have focused on micro or nano-based islet immunoisolation systems and tested the efficacy of encapsulated islets using in vitro and in vivo platforms. In this review, we address current progress and obstacles for the development of a bioartificial pancreas using micro/nano-based systems for encapsulation of islets.
  • Placeholder
    PublicationMetadata only
    Detection of interaction constants between biological clock proteins by Surface Plasmon Resonance
    (AIChE, 2012) Çakır, Bilal; Department of Chemical and Biological Engineering; Department of Chemical and Biological Engineering; Department of Chemical and Biological Engineering; Department of Chemical and Biological Engineering; N/A; Department of Chemical and Biological Engineering; Kızılel, Seda; Kavaklı, İbrahim Halil; Gidon, Doğan; Asımgil, Hande; Kızılel, Rıza; Kepsütlü, Burcu; Demirer, Gözde Sultan; Faculty Member; Faculty Member; Undergraduated Student; PhD Student; Researcher; Master Student; Undergraduated Student; Department of Chemical and Biological Engineering; College of Engineering; College of Engineering; College of Engineering; Graduate School of Sciences and Engineering; College of Engineering; Graduate School of Sciences and Engineering; College of Engineering; 28376; 40319; N/A; N/A; 114475; N/A; N/A
    Organisms adopt their behaviors and physiology to the appropriate time of the day to anticipate daily environmental changes and the circadian clock regulates their daily rhythms. In mammals, the clock is present in essentially every cell. A heterodimer of CLOCK and BMAL1 proteins binds to the E-box in Per and Cry promoters and activates their transcription. In this work, we have purified core clock proteins and characterized the affinity of previously identified clock-relevant transcription factors. We have investigated the mechanism of the clock complex and the interactions of clock proteins with and without DNA using Surface Plasmon Resonance (SPR). Kinetic parameters determined from real time data bring a solid insight into the interactions of the clock proteins with their cognate promoter.