In:
ChemBioChem, Wiley, Vol. 4, No. 2-3 ( 2003-03-03), p. 147-154
Abstract:
Tetraantennary peptides [glycine n ‐NHCH 2 ] 4 C can form stable noncovalent structures by self‐assembly through intermolecular hydrogen bonding. The oligopeptide chains assemble as polyglycine II to yield submicron‐sized, flat, one‐molecule‐thick sheets. Attachment of α ‐ N ‐acetylneuraminic acid (Neu5Ac α ) to the terminal glycine residues gives rise to water‐soluble assembled glycopeptides that are able to bind influenza virus multivalently and inhibit adhesion of the virus to cells 10 3 ‐fold more effectively than a monomeric glycoside of Neu5Ac α. Another antiviral strategy based on virus‐promoted assembly of the glycopeptides was also demonstrated. Consequently, the self‐assembly principle offers new perspectives on the design of multivalent antivirals.
Type of Medium:
Online Resource
ISSN:
1439-4227
,
1439-7633
DOI:
10.1002/cbic.200390025
Language:
English
Publisher:
Wiley
Publication Date:
2003
detail.hit.zdb_id:
2020469-3
SSG:
12
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