Multiple glycosylation of de novo designed α-helical coiled coil peptides

Falenski, Jessica A.; Gerling, Ulla I. M.; Koksch, Beate

doi:10.1016/j.bmc.2010.03.061

Cited by 13 publications

(18 citation statements)

References 12 publications

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“…This suggests that TF-antigen interferes with formation of the hydrogen bond pattern of an ␣-helix, which is most likely attributable to steric hindrance. The calculated van der Waals volume of the Ser side chain is increased from 26.1 to 168.7 Å due to the presence of a single carbohydrate moiety (56,57).…”

Section: Resultsmentioning

confidence: 98%

Discovery of Novel Inhibitors of a Disintegrin and Metalloprotease 17 (ADAM17) Using Glycosylated and Non-glycosylated Substrates

Minond

Čudić

Bionda

et al. 2012

Journal of Biological Chemistry

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Section: Resultsmentioning

confidence: 98%

Discovery of Novel Inhibitors of a Disintegrin and Metalloprotease 17 (ADAM17) Using Glycosylated and Non-glycosylated Substrates

Minond

Čudić

Bionda

et al. 2012

Journal of Biological Chemistry

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“…Coiled-coil motifs are common among natural proteins, in fact, sequence analysis has shown that nearly 2–3% of natural proteins contain coiled-coils (Wolf et al, 1997; Burkhard et al, 2001). The coiled-coil consists of two to seven α-helical strands that form a left-handed superhelical twist (Woolfson, 2005; Falenski et al, 2010). Its amino acid sequence is characterized by a seven residue periodicity, called a heptad repeat and enables the rational design by modification, for example with carbohydrate or peptide ligands (Zacco et al, 2015a,b).…”

Section: Neurogenesis Inducing Biomaterialsmentioning

confidence: 99%

Self-Assembling Peptides as Extracellular Matrix Mimics to Influence Stem Cell's Fate

Hellmund

Koksch

2019

Front. Chem.

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Interest in biologically active materials that can be used as cell culture substrates for medicinal applications has increased dramatically over the last decade. The design and development of biomaterials mimicking the natural environment of different cell types, the so-called extracellular matrix (ECM), is the focus of research in this field. The ECM exists as an ensemble of several adhesion proteins with different functionalities that can be presented to the embedded cells. These functionalities regulate numerous cellular processes. Therefore, different approaches and strategies using peptide- and protein-based biopolymers have been investigated to support the proliferation, differentiation, and self-renewal of stem cells, in the context of regenerative medicine. This minireview summarizes recent developments in this area, with a focus on peptide-based biomaterials used as stem cell culture substrates.

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“…In that study, the non-glycosylated peptide is helical, but the addition of a monosaccharide disrupts the helicity, and increasing the carbohydrate size to a disaccharide leads to further decreases in helicity (although the glycopeptides remain active). Other work showed that glycosylation appears to only have a minimal effect on the helical nature of α-helical (Palian et al, 2003 ; Li et al, 2014b ) and coiled coil glycopeptides (Falenski et al, 2010 ), and in some cases may stabilize the peptide's tertiary structure (Andersson et al, 1998 ). Therefore, when a helical system is required in a peptide, studies must be made on a case-by-case basis to determine if glycosylation will affect the peptide secondary structure.…”

Section: Benefits and Disadvantages Of Carbohydrate Incorporationmentioning

confidence: 99%

CNS active O-linked glycopeptides

Jones

Polt

2015

Front. Chem.

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Naturally occurring glycopeptides and glycoproteins play important roles in biological processes. Glycosylation is one of the most common post-translational modifications in vivo. Glycopeptides are involved in cell signaling and sorting, providing cell surface markers for recognition. From the drug design and synthesis perspective, modification of a peptide through glycosylation results in increased bioavailability and bioactivity of glycopeptides in living systems with negligible toxicity of degradation products. Glycopeptide synthesis can be accomplished through incorporation of a glycosylated amino acid in solid phase peptide synthesis (SPPS) to form the desired peptide, or via incorporation of sugar-amino acid moieties. Additionally, research indicates that glycosylation increases penetration of the blood-brain barrier (BBB) by peptides, which may lead to novel therapeutics for neurological disorders. Recent applications of glycopeptides have focused on the in vivo central nervous system (CNS) effects after peripheral administration of centrally active peptides modified with various carbohydrates.

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Multiple glycosylation of de novo designed α-helical coiled coil peptides

Cited by 13 publications

References 12 publications

Discovery of Novel Inhibitors of a Disintegrin and Metalloprotease 17 (ADAM17) Using Glycosylated and Non-glycosylated Substrates

Discovery of Novel Inhibitors of a Disintegrin and Metalloprotease 17 (ADAM17) Using Glycosylated and Non-glycosylated Substrates

Self-Assembling Peptides as Extracellular Matrix Mimics to Influence Stem Cell's Fate

CNS active O-linked glycopeptides

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