Engineering Complementary Hydrophobic Interactions to Control β‑Hairpin Peptide Self-Assembly, Network Branching, and Hydrogel Properties

The MAX1 β-hairpin peptide (VKVK­VKVK-VDPPT-KVKV­KVKV-NH2) has been shown to form nanofibrils having a cross-section of two folded peptides forming a hydrophobic, valine-rich core, and the polymerized fibril exhibits primarily β-sheet hydrogen bonding. − These nanofibrils form hydrogel networks thro...

Ausführliche Beschreibung

Bibliographische Detailangaben

Veröffentlicht in:	Biomacromolecules 2014-11, Vol.15 (11), p.3891-3900
Hauptverfasser:	Sathaye, Sameer, Zhang, Huixi, Sonmez, Cem, Schneider, Joel P, MacDermaid, Christopher M, Von Bargen, Christopher D, Saven, Jeffery G, Pochan, Darrin J
Format:	Artikel
Sprache:	eng
Schlagworte:	Agronomy. Soil science and plant productions Biological and medical sciences Chemical Engineering - methods Fundamental and applied biological sciences. Psychology Genetics and breeding of economic plants Hydrogels - chemistry Hydrogels - metabolism Hydrophobic and Hydrophilic Interactions Peptide Fragments - chemistry Peptide Fragments - metabolism Plant breeding: fundamental aspects and methodology Protein Folding Protein Structure, Secondary Protein Structure, Tertiary
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!