Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Direct observation of time-resolved polymorphic states in the self-assembly of end-capped heptapeptides.

Literature DB >> 21538748

Direct observation of time-resolved polymorphic states in the self-assembly of end-capped heptapeptides.

Jozef Adamcik¹, Valeria Castelletto, Sreenath Bolisetty, Ian W Hamley, Raffaele Mezzenga.

Abstract

Mesh：

Substances：

Year: 2011 PMID： 21538748 DOI： 10.1002/anie.201100807

Source DB: PubMed Journal: Angew Chem Int Ed Engl ISSN： 1433-7851 Impact factor: 15.336

Keyword Cloud
Cited

× No keyword cloud information.

21 in total

1. A kinetic study of ovalbumin fibril formation: the importance of fragmentation and end-joining.

Authors: Jason M D Kalapothakis; Ryan J Morris; Juraj Szavits-Nossan; Kym Eden; Sam Covill; Sean Tabor; Jay Gillam; Perdita E Barran; Rosalind J Allen; Cait E MacPhee
Journal: Biophys J Date: 2015-05-05 Impact factor: 4.033

2. Critical Influence of Cosolutes and Surfaces on the Assembly of Serpin-Derived Amyloid Fibrils.

Authors: Michael W Risør; Dennis W Juhl; Morten Bjerring; Joachim Mathiesen; Jan J Enghild; Niels C Nielsen; Daniel E Otzen
Journal: Biophys J Date: 2017-08-08 Impact factor: 4.033

3. Coexistence of ribbon and helical fibrils originating from hIAPP(20-29) revealed by quantitative nanomechanical atomic force microscopy.

Authors: Shuai Zhang; Maria Andreasen; Jakob T Nielsen; Lei Liu; Erik H Nielsen; Jie Song; Gang Ji; Fei Sun; Troels Skrydstrup; Flemming Besenbacher; Niels C Nielsen; Daniel E Otzen; Mingdong Dong
Journal: Proc Natl Acad Sci U S A Date: 2013-02-06 Impact factor: 11.205

Direct observation of time-resolved polymorphic states in the self-assembly of end-capped heptapeptides.

1. A kinetic study of ovalbumin fibril formation: the importance of fragmentation and end-joining.

2. Critical Influence of Cosolutes and Surfaces on the Assembly of Serpin-Derived Amyloid Fibrils.

3. Coexistence of ribbon and helical fibrils originating from hIAPP(20-29) revealed by quantitative nanomechanical atomic force microscopy.

4. Tuning nanostructure dimensions with supramolecular twisting.

Review 5. Protein nanofibrils and their use as building blocks of sustainable materials.

6. Self-assembly mechanisms of nanofibers from peptide amphiphiles in solution and on substrate surfaces.

7. Supramolecular Polymers Formed by ABC Miktoarm Star Peptides.

8. Plasmonic Chirality Imprinting on Nucleobase-Displaying Supramolecular Nanohelices by Metal-Nucleobase Recognition.

Review 9. Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology.

10. Tuning self-assembled nanostructures through enzymatic degradation of a peptide amphiphile.