Browsing by Author "Khan, Anooshay"

Now showing 1 - 5 of 5

Open Access
Combating infectious diseases with synthetic biology
(American Chemical Society, 2022-01-25) Khan, Anooshay; Ostaku, Julian; Aras, Ebru; Safak Seker, Urartu Ozgur
Over the past decades, there have been numerous outbreaks, including parasitic, fungal, bacterial, and viral infections, worldwide. The rate at which infectious diseases are emerging is disproportionate to the rate of development for new strategies that could combat them. Therefore, there is an increasing demand to develop novel, specific, sensitive, and effective methods for infectious disease diagnosis and treatment. Designed synthetic systems and devices are becoming powerful tools to treat human diseases. The advancement in synthetic biology offers efficient, accurate, and cost-effective platforms for detecting and preventing infectious diseases. Herein we focus on the latest state of living theranostics and its implications.
Open Access
Design and construction of protein and peptide-based self-assembled nanostructures
(Elsevier, 2022-01-01) Yuca, Esra; Khan, Anooshay; Hacıosmanoğlu, Nedim; Şeker, Urartu Özgür Şafak; Pandya, A.; Singh, V.; Bhosale, R. S.
Self-assembly is the driving force for the formation of biological materials. From nucleic acid conformations to more complex cellular organizations, self-assembling structures shape biological functionality. So, the design of self-assembling biomolecular structures holds a great advantage for enhanced material properties. In biological processes, inorganic structures are created in a hierarchical fashion utilizing biomolecule-based templates. Since they have recognition and self-assembly properties, biomolecules can control highly organized inorganic material formation in nature. The bio-templating approach takes advantage of biomolecules’ self-assembly properties to develop new nanostructures with superior chemical and physical properties. Here, peptides and proteins including β-sheets, β-hairpins, α-helix, amyloid, capsid, ferritin, and albumin, used in the formation of nanostructures with desired functionality under mild environmental conditions, and their applications are discussed.
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Designed for Turkey, built in Pakistan : Kocatepe & Faisal Mosques
(Bilkent University, 2015) Adeeb, Ali Haider; Khan, Anooshay; Khan, Haziq; Quddus, Nasir; Abedee, Zayan
Open Access
Highly potent peptide therapeutics to prevent protein aggregation in huntington’s disease
(American Chemical Society, 2023-12-14) Khan, Anooshay; Özçelik, Cemile Elif; Begli, Özge; Oğuz, Oğuzhan; Kesici, M. S.; Kasırga, Talip Serkan; Özçubukcu, S.; Yuca, E.; Şeker, Urartu Özgür Şafak
Huntington’s disease (HD) is a neurodegenerative disorder resulting from a significant amplification of CAG repeats in exon 1 of the Huntingtin (Htt) gene. More than 36 CAG repeats result in the formation of a mutant Htt (mHtt) protein. These amino-terminal mHtt fragments lead to the formation of misfolded proteins, which then form aggregates in the relevant brain regions. Therapies that can delay the progression of the disease are imperative to halting the course of the disease. Peptide-based drug therapies provide such a platform. Inhibitory peptides were screened against monomeric units of both wild type (Htt(Q25)) and mHtt fragments, Htt(Q46) and Htt(Q103). Fibril kinetics was studied by utilizing the Thioflavin T (ThT) assay. Atomic force microscopy was also used to study the influence of the peptides on fibril formation. These experiments demonstrate that the chosen peptides suppress the formation of fibrils in mHtt proteins and can provide a therapeutic lead for further optimization and development.
Open Access
Peptide therapeutics to prevent protein aggregation in Huntington’s disease
(2022-09) Khan, Anooshay
Huntington’s disease is a progressive, autosomal dominant neurodegenerative disease caused by dramatic CAG repeat expansion in exon 1 of the Huntington (HTT) gene. More than 36 CAG repeats lead to the generation of mutant HTT (mHTT) fragments. These amino-terminal mutant HTT fragments result in misfolded proteins that give rise to oligomers and subsequent aggregate formation in relevant brain areas. Available therapies mainly focus on ameliorating the symptoms of the disease. Therefore, therapeutic interventions which can delay the onset of disease are imperative for halting disease progression. Peptide-based drug therapy provide such a platform. Previously in our lab, candidate ligand peptides were screened against both willd type (Htt-Q25) and mHTT fragments such as Htt-Q46, and Htt-Q103. This was done using different display technologies This work focuses on the in vitro characterization of those selected peptides. Fibril formation was observed in real-time using Thiofllavin T assay. Selected peptides were added to check their effect on fibril formation by change in fluorescence signal. The effect of peptides on fibril formation was also studied using Atomic Force microscopy. 3 of the 6 selected peptides (HHGANSLSLVSQD), (HGLHSMHNKLTR) and (WMFPSLKLLDYH) successfully showed a blocking in aggregation. These studies show that the selected peptides are affective for inhibiting the aggregation of fibrils in mHTT proteins.