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ADS-J1 disaggregates semen-derived amyloid fibrils

Jinqing Li1, Zichao Yang1, Han Liu1

  • 1Guangdong Provincial Key Laboratory of New Drug Screening, School of Pharmaceutical Sciences, Southern Medical University, Guangzhou 510515, Guangdong Province, China.

The Biochemical Journal
|March 17, 2019
PubMed

Insights

ADS-J1 effectively disassembles semen-derived amyloid fibrils (SEVI) and other amyloid structures. This compound shows potential as a dual-action microbicide and a therapeutic for amyloid diseases.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Drug Discovery

Background:

  • Semen-derived amyloid fibrils (SEVI) enhance HIV-1 sexual transmission.
  • ADS-J1 inhibits HIV-1 entry and seminal amyloid fibril formation.
  • The effect of ADS-J1 on mature seminal fibrils was previously unknown.

Purpose of the Study:

  • To investigate ADS-J1's capacity to disassemble seminal amyloid fibrils.
  • To elucidate the mechanism of action for ADS-J1's fibril remodeling.
  • To explore ADS-J1's potential as a microbicide and therapeutic for amyloid diseases.

Main Methods:

  • Biophysical and biochemical measurements.
  • Molecular dynamic (MD) simulations.
  • Analysis of fibril remodeling of SEVI, SEM1, and endogenous seminal fibrils.

Main Results:

  • ADS-J1 effectively remodeled SEVI, SEM186-107, and endogenous seminal fibrils.
  • ADS-J1 disaggregated SEVI fibrils into monomers, independent of oxidation.
  • MD simulations showed ADS-J1 binds strongly to PAP248-286, leading to disassembly and preventing re-aggregation.

Conclusions:

  • ADS-J1 disassembles seminal amyloid fibrils and other amyloid structures like Aβ1-42.
  • ADS-J1's mechanism involves binding to the fibril surface and core, inducing conformational changes.
  • ADS-J1 holds promise as a combination microbicide and a lead compound for amyloidogenic diseases.
Keywords:
HIVSEVIamyloiddisaggregatemolecular dynamics

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