Show/Hide Menu
Hide/Show Apps
Logout
Türkçe
Türkçe
Search
Search
Login
Login
OpenMETU
OpenMETU
About
About
Open Science Policy
Open Science Policy
Open Access Guideline
Open Access Guideline
Postgraduate Thesis Guideline
Postgraduate Thesis Guideline
Communities & Collections
Communities & Collections
Help
Help
Frequently Asked Questions
Frequently Asked Questions
Guides
Guides
Thesis submission
Thesis submission
MS without thesis term project submission
MS without thesis term project submission
Publication submission with DOI
Publication submission with DOI
Publication submission
Publication submission
Supporting Information
Supporting Information
General Information
General Information
Copyright, Embargo and License
Copyright, Embargo and License
Contact us
Contact us
Peptide stapling by late-stage Suzuki-Miyaura cross-coupling
Download
1860-5397-18-1.pdf
Date
2022-01-01
Author
Gruss, Hendrik
Feiner, Rebecca C.
Mseya, Ridhiwan
Schroeder, David C.
Jewginski, Michat
Mueller, Kristian M.
Latajka, Rafat
Marıon, Antoıne
Sewald, Norbert
Metadata
Show full item record
This work is licensed under a
Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License
.
Item Usage Stats
191
views
65
downloads
Cite This
The development of peptide stapling techniques to stabilise alpha-helical secondary structure motifs of peptides led to the design of modulators of protein-protein interactions, which had been considered undruggable for a long time. We disclose a novel approach towards peptide stapling utilising macrocyclisation by late-stage Suzuki-Miyaura cross-coupling of bromotryptophan-containing peptides of the catenin-binding domain of axin. Optimisation of the linker length in order to find a compromise between both sufficient linker rigidity and flexibility resulted in a peptide with an increased alpha-helicity and enhanced binding affinity to its native binding partner beta-catenin. An increased proteolytic stability against proteinase K has been demonstrated.
Subject Keywords
accelerated molecular dynamics
,
halotryptophan
,
intrinsically disordered peptides
,
late-stage diversification
,
macrocyclisation
,
molecular dynamics
,
stapled peptides
,
Suzuki-Miyaura cross-coupling
,
ACCELERATED MOLECULAR-DYNAMICS
,
ALPHA-HELICAL PEPTIDES
,
ENZYMATIC HALOGENATION
,
TRYPTOPHAN
,
ARYLATION
,
MACROCYCLIZATION
,
DIVERSIFICATION
,
MILD
,
SIMULATIONS
,
STABILITY
URI
https://hdl.handle.net/11511/95357
Journal
BEILSTEIN JOURNAL OF ORGANIC CHEMISTRY
DOI
https://doi.org/10.3762/bjoc.18.1
Collections
Department of Chemistry, Article
Suggestions
OpenMETU
Core
Bioactive Surface Design Based on Functional Composite Electrospun Nanofibers for Biomolecule Immobilization and Biosensor Applications
Uzun, Sema Demirci; Kayaci, Fatma; UYAR, Tamer; TİMUR, SUNA; Toppare, Levent Kamil (2014-04-09)
The combination of nanomaterials and conducting polymers attracted remarkable attention for development of new immobilization matrices for enzymes. Hereby, an efficient surface design was investigated by modifying the graphite rod electrode surfaces with one-step electrospun nylon 6,6 nanofibers or 4% (w/w) multiwalled carbon nanotubes (MWCNTs) incorporating nylon 6,6 nanofibers (nylon 6,6/4MWCNT). High-resolution transmission electron microscopy study confirmed the successful incorporation of the MWCNTs in...
Comonomer effects on binding performances and morphology of acrylate-based imprinted polymers
Tunc, Yeliz; Hasırcı, Nesrin; Yesilada, Akgul; Ulubayram, Kezban (2006-09-20)
The objective of this study was to investigate the effect of different functional groups of molecularly imprinted polymers (MIPs) on the binding characteristics towards a specific template molecule by examining selectivity and recognition processes. Several non-covalent theophylline imprinted polymers (TIPs) were prepared by using only methacrylic acid (MAA), or MAA and 2-hydroxyethyl methacrylate (HEMA) comonomer, or MAA and acrylamide (ACM) comonomer. In all cases, a high amount of ethylene glycol dimetha...
Deactivation model for textural effects on kinetics of gas-solid noncatalytic reactions ''char gasification with CO2''
Yasyerli, N; Doğu, Timur; Dogu, G; Ar, I (1996-06-01)
Variation of the reactivity of a solid reactant due to changes in number of working active sites and pore structure was represented by a deactivation model. The model was shown to give good aggreement with the experimental data obtained for the gasification of chars of different lignites. All the kinetic data obtained at different temperatures (800 degrees-950 degrees C) and also for different types of coals were represented with a single generalized relation. The increase of the surface area of the char at...
SIMULATION CALCULATIONS FOR GOLD CLUSTERS ON THE GAAS(110) SURFACE
Erkoç, Şakir; HALICIOGLU, T; TILLER, WA (1992-08-15)
Energy- and structure-related properties of small gold clusters deposited on the GaAs(110) surface were investigated in this work using a molecular dynamics procedure. A recently developed potential energy function based on two- and three-body interactions was employed in calculating energies and forces. These calculations produced some consistent results with experiments. The three-body interactions involving As atoms in particular, were found to play an important role in determining favorable binding site...
Chemoselective Immobilization of Proteins by Microcontact Printing and Bio-orthogonal Click Reactions
Tolstyka, Zachary P.; Richardson, Wade; Bat, Erhan; Stevens, Caitlin J.; Parra, Dayanara P.; Dozier, Jonathan K.; Distefano, Mark D.; Dunn, Bruce; Maynard, Heather D. (Wiley, 2013-12-16)
Herein, a combination of microcontact printing of functionalized alkanethiols and site-specific modification of proteins is utilized to chemoselectively immobilize proteins onto gold surfaces, either by oxime- or copper-catalyzed alkyne-azide click chemistry. Two molecules capable of click reactions were synthesized, an aminooxy-functionalized alkanethiol and an azide-functionalized alkanethiol, and self-assembled monolayer (SAM) formation on gold was confirmed by IR spectroscopy. The alkanethiols were then...
Citation Formats
IEEE
ACM
APA
CHICAGO
MLA
BibTeX
H. Gruss et al., “Peptide stapling by late-stage Suzuki-Miyaura cross-coupling,”
BEILSTEIN JOURNAL OF ORGANIC CHEMISTRY
, vol. 18, pp. 0–0, 2022, Accessed: 00, 2022. [Online]. Available: https://hdl.handle.net/11511/95357.