Search

Your search keyword '"Farbiarz, Karine"' showing total 6 results
Start Over Author "Farbiarz, Karine"
6 results on '"Farbiarz, Karine"'

2. Eine Hot-Spot-Segmentstrategie zum Entwurf von Mimetika der Kreuzamyloid-Interaktionsflächen als Amyloidinhibitoren

Author

Andreetto, Erika, primary, Malideli, Eleni, additional, Yan, Li-Mei, additional, Kracklauer, Michael, additional, Farbiarz, Karine, additional, Tatarek-Nossol, Marianna, additional, Rammes, Gerhard, additional, Prade, Elke, additional, Neumüller, Tatjana, additional, Caporale, Andrea, additional, Spanopoulou, Anna, additional, Bakou, Maria, additional, Reif, Bernd, additional, and Kapurniotu, Aphrodite, additional

Published
2015
Full Text
View/download PDF

3. A Hot‐Segment‐Based Approach for the Design of Cross‐Amyloid Interaction Surface Mimics as Inhibitors of Amyloid Self‐Assembly

Author

Andreetto, Erika, primary, Malideli, Eleni, additional, Yan, Li‐Mei, additional, Kracklauer, Michael, additional, Farbiarz, Karine, additional, Tatarek‐Nossol, Marianna, additional, Rammes, Gerhard, additional, Prade, Elke, additional, Neumüller, Tatjana, additional, Caporale, Andrea, additional, Spanopoulou, Anna, additional, Bakou, Maria, additional, Reif, Bernd, additional, and Kapurniotu, Aphrodite, additional

Published
2015
Full Text
View/download PDF

4. A quantitative and site-specific chemoenzymatic glycosylation approach for PEGylated MUC1 peptides

Author

Bello, Claudia, Farbiarz, Karine, Moeller, Jan F., Becker, Christian F. W., Schwientek, Tilo, Bello, Claudia, Farbiarz, Karine, Moeller, Jan F., Becker, Christian F. W., and Schwientek, Tilo

Abstract

Full control over complex post-translational modifications (PTMs), such as O-glycosylation, is a prerequisite for testing and understanding the biological role of these modifications in protein function. Despite considerable progress over the last years, high throughput and easy-to-use methods for the synthesis of complex glycosylated peptides are still missing. We present here an efficient methodology to produce homogeneous site-specifically O-glycosylated peptides. Sequential chemoenzymatic glycosylation and separation from the reaction components are achieved via the temporary attachment of a monodisperse polyethylene glycol (PEG) polymer to the N-terminus of these peptides. Subsequent proteolytic removal of the PEG moiety allows quantitative recovery of homogeneous O-glycopeptides, suitable as building blocks for glycoprotein synthesis. Here, we demonstrate the preparation of glucuronylated variants of MUC1, a well-known member of the human mucin family. Homogeneously O-glycosylated variants were synthesized and will be used to study the role of O-linked glucuronic acid epitopes within the functional environment of the human MUC1 tandem repeat.

Published
2014

6. A Hot-Segment-Based Approach for the Design of Cross-Amyloid Interaction Surface Mimics as Inhibitors of Amyloid Self-Assembly.

Author

Andreetto E, Malideli E, Yan LM, Kracklauer M, Farbiarz K, Tatarek-Nossol M, Rammes G, Prade E, Neumüller T, Caporale A, Spanopoulou A, Bakou M, Reif B, and Kapurniotu A

Subjects
Alzheimer Disease metabolism, Amyloid beta-Peptides chemistry, Amyloid beta-Peptides metabolism, Diabetes Mellitus, Type 2 metabolism, Humans, Islet Amyloid Polypeptide chemistry, Protein Aggregates drug effects, Surface Properties, Amyloid beta-Peptides antagonists & inhibitors, Drug Design, Islet Amyloid Polypeptide pharmacology
Abstract

The design of inhibitors of protein-protein interactions mediating amyloid self-assembly is a major challenge mainly due to the dynamic nature of the involved structures and interfaces. Interactions of amyloidogenic polypeptides with other proteins are important modulators of self-assembly. Here we present a hot-segment-linking approach to design a series of mimics of the IAPP cross-amyloid interaction surface with Aβ (ISMs) as nanomolar inhibitors of amyloidogenesis and cytotoxicity of Aβ, IAPP, or both polypeptides. The nature of the linker determines ISM structure and inhibitory function including both potency and target selectivity. Importantly, ISMs effectively suppress both self- and cross-seeded IAPP self-assembly. Our results provide a novel class of highly potent peptide leads for targeting protein aggregation in Alzheimer's disease, type 2 diabetes, or both diseases and a chemical approach to inhibit amyloid self-assembly and pathogenic interactions of other proteins as well., (© 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)

Published
2015
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results