1.
Biochemistry
; 50(13): 2381-3, 2011 Apr 05.
Artículo
en Inglés
| MEDLINE
| ID: mdl-21375275
RESUMEN
Introduction of a cationic residue at the N-terminus and an aromatic residue at the C-terminus of a collagen-related peptide can generate favorable cation-π interactions between the termini of collagen triple helices. The experimental results indicate that such cation-π interactions can promote the self-assembly of collagen triple helices into a higher-order structure in a head-to-tail manner. Our current work shows that cation-π interactions can serve as an effective force in preparing collagen-related biomaterials.