M. Guerrini

Pentosan polysulfate inhibits attachment and infection by SARS-CoV-2 in vitro: insights into structural requirements for binding.

This study shows that pentosan polysulfate inhibits SARS-CoV-2 attachment and infection in vitro, with effectiveness comparable to heparin and better than low molecular weight heparin.

Glycosaminoglycans induce conformational change in the SARS-CoV-2 Spike S1 Receptor Binding Domain.

This study shows that various glycosaminoglycans, beyond heparin, can induce conformational changes in the SARS-CoV-2 Spike S1 receptor binding domain.

SARS-CoV-2 Spike S1 Receptor Binding Domain undergoes Conformational Change upon Interaction with Low Molecular Weight Heparins.

This study shows low molecular weight heparins induce conformational changes in SARS-CoV-2 Spike RBD, suggesting potential for repurposing as antiviral agents.

Heparin inhibits cellular invasion by SARS-CoV-2: structural dependence of the interaction of the surface protein (spike) S1 receptor binding domain with heparin.

This study shows heparin inhibits SARS-CoV-2 invasion by binding to the Spike protein's RBD and inducing conformational changes, with structural features of heparin playing a key role.

The 2019 coronavirus (SARS-CoV-2) surface protein (Spike) S1 Receptor Binding Domain undergoes conformational change upon heparin binding.

The paper shows that SARS-CoV-2 Spike S1 RBD undergoes a conformational change when bound to heparin, suggesting potential for heparin as a therapeutic.

Analysis of solid-state heparin samples by ATR-FTIR spectroscopy

This paper proposes using ATR-FTIR spectroscopy with multivariate analysis to rapidly and cost-effectively monitor heparin purity and detect contaminants.

Using ATR-FTIR spectroscopy to characterise crude heparin samples by composition and structural features.

This paper uses ATR-FTIR spectroscopy with chemometric analysis to characterize crude heparin samples by composition and structural features, enabling quality control during production.

A glycosaminoglycan extract from Portunus pelagicus inhibits BACE1, the β secretase implicated in Alzheimer’s disease

This study identifies a marine-derived glycosaminoglycan extract from Portunus pelagicus that inhibits BACE1 with reduced anticoagulant activity compared to mammalian heparin.