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Nanostructures from the self-assembly of -helical peptide amphiphiles.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Meng, Qingbin Kou, Yingying Ma, Xin Guo, Lei Liu, Keliang
Description	Country affiliation: China Author Affiliation: Meng Q ( Beijing Institute of Pharmacology and Toxicology, Beijing, 100850, China.)
Abstract	Self-assembly of PAs composed of palmitic acid and several repeated heptad peptide sequences, C15H31CO-(IEEYTKK)(n)-NH2 (n = 1-4, represented by PA1-PA4), was investigated systematically. The secondary structures of the PAs were characterized by CD. PA3 and PA4 (n = 3 and 4, respectively) showed an -helical structure, whereas PA1 and PA2 (n = 1 and 2, respectively) did not display an -helical conformations under the tested conditions. The morphology of the self-assembled peptides in aqueous medium was studied by transmission electron microscopy. As the number of heptad repeats in the PAs increased, the nanostructure of the self-assembled peptides changed from nanofibers to nanovesicles. Changes of the secondary structures and the self-assembly morphologies of PA3 and PA4 in aqueous medium with various cations were also studied. The critical micelle concentrations were determined using a pyrene fluorescence probe. In conclusion, this method may be used to design new peptide nanomaterials.
File Format	HTM / HTML
ISSN	10752617
Issue Number	3
Journal	Journal of Peptide Science
Volume Number	20
e-ISSN	10991387
Language	English
Publisher	Wiley
Publisher Date	2014-03-01
Publisher Place	Great Britain (UK)
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Biochemistry Nanostructures Chemistry Peptides Hydrophobic And Hydrophilic Interactions Protein Structure, Secondary Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Structural Biology Medicine Drug Discovery Biochemistry Molecular Biology Pharmacology Molecular Medicine

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