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7 results on '"Kracklauer, Michael"'

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
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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
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4. Selektiv N-methylierte lösliche IAPP-Mimetika als potente IAPP-Rezeptoragonisten und nanomolare Inhibitoren der Selbstassoziation von IAPP und Aβ40

Author

Yan, Li-Mei, primary, Velkova, Aleksandra, additional, Tatarek-Nossol, Marianna, additional, Rammes, Gerhard, additional, Sibaev, Andrei, additional, Andreetto, Erika, additional, Kracklauer, Michael, additional, Bakou, Maria, additional, Malideli, Eleni, additional, Göke, Burkhard, additional, Schirra, Jörg, additional, Storr, Martin, additional, and Kapurniotu, Aphrodite, additional

Published
2013
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5. Selectively N-Methylated Soluble IAPP Mimics as Potent IAPP Receptor Agonists and Nanomolar Inhibitors of Cytotoxic Self-Assembly of Both IAPP and Aβ40

Author

Yan, Li-Mei, primary, Velkova, Aleksandra, additional, Tatarek-Nossol, Marianna, additional, Rammes, Gerhard, additional, Sibaev, Andrei, additional, Andreetto, Erika, additional, Kracklauer, Michael, additional, Bakou, Maria, additional, Malideli, Eleni, additional, Göke, Burkhard, additional, Schirra, Jörg, additional, Storr, Martin, additional, and Kapurniotu, Aphrodite, additional

Published
2013
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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
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7. Selectively N-methylated soluble IAPP mimics as potent IAPP receptor agonists and nanomolar inhibitors of cytotoxic self-assembly of both IAPP and Aβ40.

Author

Yan LM, Velkova A, Tatarek-Nossol M, Rammes G, Sibaev A, Andreetto E, Kracklauer M, Bakou M, Malideli E, Göke B, Schirra J, Storr M, and Kapurniotu A

Subjects
Amino Acid Sequence, Amyloid metabolism, Amyloid ultrastructure, Amyloid beta-Peptides antagonists & inhibitors, Amyloid beta-Peptides metabolism, Amyloid beta-Peptides ultrastructure, Humans, Islet Amyloid Polypeptide metabolism, Islet Amyloid Polypeptide ultrastructure, Methylation, Molecular Sequence Data, Peptide Fragments antagonists & inhibitors, Peptide Fragments metabolism, Peptide Fragments ultrastructure, Receptors, Islet Amyloid Polypeptide metabolism, Amylin Receptor Agonists, Amyloid antagonists & inhibitors, Islet Amyloid Polypeptide chemistry, Peptidomimetics chemistry, Peptidomimetics pharmacology
Published
2013
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