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Peptides derived from HIV-1 gp120 co-receptor binding domain form amyloid fibrils and enhance HIV-1 infection.

FEBS letters (2014-03-25)
Suiyi Tan, Lin Li, Lu Lu, Chungen Pan, Hong Lu, Yelena Oksov, Xiaojuan Tang, Shibo Jiang, Shuwen Liu
ABSTRACT

Amyloid fibrils play important roles in HIV-1 infection. We found peptides derived from the HIV-1 gp120 co-receptor binding region, which are defined as enhancing peptides (EPs), could form amyloid fibrils and remarkably enhance HIV-1 infection. EPs bound to the virus and promoted the interaction between HIV-1 and target cells. The antiviral efficacy of antiretroviral drugs (ARVs) was substantially impaired in the presence of EPs. Epigallocatechin gallate (EGCG) could both inhibit the formation of fibrils composed of EPs and counteract the EP-mediated enhancement of HIV-1 infection. Our findings identify viral derived amyloid fibrils that hold potential for biochemical applications.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
(−)-Epigallocatechin gallate, ≥95%
Sigma-Aldrich
(−)-Epicatechin, ≥90% (HPLC)
Supelco
(+)-Catechin, analytical standard
Sigma-Aldrich
(−)-Epigallocatechin gallate, ≥80% (HPLC), from green tea
Sigma-Aldrich
(−)-Epicatechin, ≥98% (HPLC), from green tea
Supelco
Epigallocatechin gallate, Pharmaceutical Secondary Standard; Certified Reference Material
Supelco
(−)-Epicatechin, analytical standard
Supelco
(−)-Epigallocatechin gallate, analytical standard
Epicatechin, primary reference standard
(±)-Catechin hydrate, primary reference standard
Epigallocatechin gallate, primary reference standard