In:
FEBS Letters, Wiley, Vol. 592, No. 13 ( 2018-07), p. 2361-2377
Abstract:
HIV ‐1 transmembrane protein gp41 plays a crucial role by forming a stable six‐helix bundle during HIV entry. Due to highly conserved sequence of gp41, the development of an effective and safe small‐molecule compound targeting gp41 is a good choice. Currently, natural polyanionic ingredients with anti‐ HIV activities have aroused concern. Here, we first discovered that a glycosylated dihydrochalcone, trilobatin, exhibited broad anti‐ HIV ‐1 activity and low cytotoxicity in vitro . Site‐directed mutagenesis analysis suggested that the hydrophobic residue (I564) located in gp41 pocket‐forming site is pivotal for anti‐ HIV activity of trilobatin. Furthermore, trilobatin displayed synergistic anti‐ HIV activities combined with other antiretroviral agents. Trilobatin has a good potential to be developed as a small‐molecule HIV ‐1 entry inhibitor for clinical combination therapy.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1002/feb2.2018.592.issue-13
DOI:
10.1002/1873-3468.13113
Language:
English
Publisher:
Wiley
Publication Date:
2018
detail.hit.zdb_id:
1460391-3
SSG:
12