lactoferrin and phenylacetic-acid

lactoferrin has been researched along with phenylacetic-acid* in 1 studies

Other Studies

1 other study(ies) available for lactoferrin and phenylacetic-acid

Article	Year
Different protein-binding selectivities for N-acyl heparin derivatives having N-phenylacetyl and heterocycle analogs of N-phenylacetyl substituted in place of N-sulfo groups. Bioorganic & medicinal chemistry letters, 2007, Jan-15, Volume: 17, Issue:2 Replacing N-sulfo groups in heparin with N-arylacyl moieties has been shown to afford charge-reduced heparin derivatives that maintain affinity for select heparin-binding proteins. In this study 50% and 100% N-desulfonated heparins were selectively N-acylated with phenylacetic acid and four phenylacetic acid analogs where the phenyl ring was replaced by a heterocycle. Protein-binding studies reveal that structural differences in the ring systems of the N-acyl groups appended to heparin afford significant affects on affinity and selectivity for different heparin-binding proteins. Topics: Acylation; Animals; Binding, Competitive; Blood Coagulation; Carbohydrate Sequence; Heparin; Heterocyclic Compounds; Humans; In Vitro Techniques; Lactoferrin; Mice; Molecular Sequence Data; Partial Thromboplastin Time; Phenylacetates; Protein Binding; Structure-Activity Relationship; Trinitrobenzenesulfonic Acid	2007

Article

Year

Different protein-binding selectivities for N-acyl heparin derivatives having N-phenylacetyl and heterocycle analogs of N-phenylacetyl substituted in place of N-sulfo groups.

Bioorganic & medicinal chemistry letters, 2007, Jan-15, Volume: 17, Issue:2

Replacing N-sulfo groups in heparin with N-arylacyl moieties has been shown to afford charge-reduced heparin derivatives that maintain affinity for select heparin-binding proteins. In this study 50% and 100% N-desulfonated heparins were selectively N-acylated with phenylacetic acid and four phenylacetic acid analogs where the phenyl ring was replaced by a heterocycle. Protein-binding studies reveal that structural differences in the ring systems of the N-acyl groups appended to heparin afford significant affects on affinity and selectivity for different heparin-binding proteins.

Topics: Acylation; Animals; Binding, Competitive; Blood Coagulation; Carbohydrate Sequence; Heparin; Heterocyclic Compounds; Humans; In Vitro Techniques; Lactoferrin; Mice; Molecular Sequence Data; Partial Thromboplastin Time; Phenylacetates; Protein Binding; Structure-Activity Relationship; Trinitrobenzenesulfonic Acid

2007