Position and orientation of gallated proanthocyanidins in lipid bilayer membranes: influence of polymerization degree and linkage type. Issue 11 (18th August 2018)

• Record Type: Journal Article
• Authors: Zhu, Wei; Khalifa, Ibrahim; Peng, Jinming; Li, Chunmei
• Is Part Of: Journal of biomolecular structure & dynamics. Volume 36:Issue 11(2018)
• Page Start: 2862
• Page End: 2875
• Publication Date: 2018-08-18
• Subjects: gallated proanthocyanidins -- polymerization degree -- linkage type -- molecular dynamic simulation -- lipid bilayer; Epigallocatechin-3-gallate-(4β→8, 2β→O→7)-epigallocatechin-3-gallate, A-type EGCG dimer -- Epigallocatechin-3-gallate-(4β→8, 2β→O→7)-epigallocatechin-3-gallate-(4β→8, 2β→O→7)-epigallocatechin-3-gallate, A-type EGCG trimer -- Epigallocatechin-3-gallate-(4β→8)-epigallocatechin-3-gallate, B-type EGCG dimer -- Epigallocatechin-3-gallate-(4β→8)-epigallocatechin-3-gallate-(4β→8)-epigallocatechin-3-gallate, B-type EGCG trimer -- Center of Mass, COM -- Degree of Polymerization, DP -- Epigallocatechin-3-gallate, EGCG -- Molecular dynamics, MD -- 1-palmitoyl-2-oleoyl phosphatidylcholine, POPC -- 1-palmitoyl-2-oleoyl phosphatidylethanolamine, POPE -- Proanthocyanidins, PAs; Biomolecules -- Periodicals; Molecular structure -- Periodicals; Molecular Biology -- Periodicals; Biomechanics -- Periodicals; 572
• DOI: 10.1080/07391102.2017.1369163
• Languages: English
• ISSNs: 0739-1102

Abstract

Abstract : It is well known that the biological activity of gallated proanthocyanidins (PAs) is highly structure-dependent. Polymerization degree (DP) and linkage types affect their biological activity greatly. Positions and orientations of gallated PAs in lipid bilayer reveal their structure-function activity at the molecular level. The present work aimed at determining the locations and orientations of epigallocatechin-3-gallate (EGCG) and its derivatives: A-type and B-type EGCG dimers and trimers in 1-palmitoyl-2-oleoyl phosphatidylcholine (POPC) and 1-palmitoyl-2-oleoyl phosphatidylethanolamine (POPE) lipid bilayer via molecular dynamic (MD) simulations. The results showed that EGCG and its derivatives localized in the lipid bilayer or on the bilayer/water interface. Their penetration depths and orientations depended on both DP and linkage types. The penetration depths decreased with the increase of DP, sequencing to be EGCG > EGCG dimers > EGCG trimers. Spatially stretched A-type PAs could form more hydrogen bonds (H-bonds) with deep oxygen atoms of lipid bilayer and have higher affinity to the lipid bilayer than B-type PAs. Our results will provide an explicit evidence for PAs' distinct biological activities.