3D Networks from Self-Assembling Ionic-Complementary Octa-Peptides

Autor:	Aline F. Miller, Alberto Saiani, Amran Mohammed
Rok vydání:	2007
Předmět:	Alanine chemistry.chemical_classification Materials science Polymers and Plastics Scattering Organic Chemistry Ionic bonding Peptide Radius Condensed Matter Physics Small-angle neutron scattering Crystallography chemistry Self-healing hydrogels Materials Chemistry Self-assembly
Zdroj:	Macromolecular Symposia. 251:88-95
ISSN:	1521-3900 1022-1360
Popis:	The self-assembly and gelation properties of a set of four octo-peptides AEAEAKAK, AEAKAEAK, FEFEFKFK and FEFKFEFK based on alanine (A), phenylalanine (F), lysine (K) and glutamic acid (E) were investigated via small angle neutron scattering (SANS). The SANS experiments suggest that AEAKAEAK peptide does not self-assemble in solution while AEAEAKAK form rod-like structure i.e.: fibres with a radius of ∼3.3 nm. The latter peptide does not form a gel suggesting that the fibres do not aggregate and form a three-dimensional network. On the other hand FEFEFKFK and FEFKFEFK peptides were found to form gels for concentrations higher than ∼7 mg ml−1. Below the critical gelation concentration these peptides were also found to form fibrillar structures with smaller average radii of ∼1.7 nm. Above the critical gelation concentration a scattering maximum is observed in the scattered intensity curve. From the position of the maximum a rough estimation of the mesh size of the gel network could be derived and was found to vary between 15 and 30 nm depending on the gel concentration.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::0768ee9249260110793dcf02b2ee48fa https://doi.org/10.1002/masy.200750512 Zobrazit plný text záznamu Plný text