INTERACTIONS OF HYALURONAN (HYALURONIC-ACID) WITH PHOSPHOLIPIDS AS DETERMINED BY GEL-PERMEATION CHROMATOGRAPHY, MULTI-ANGLE LASER-LIGHT-SCATTERING PHOTOMETRY AND H-1-NMR SPECTROSCOPY
INTERACTIONS OF HYALURONAN (HYALURONIC-ACID) WITH PHOSPHOLIPIDS AS DETERMINED BY GEL-PERMEATION CHROMATOGRAPHY, MULTI-ANGLE LASER-LIGHT-SCATTERING PHOTOMETRY AND H-1-NMR SPECTROSCOPY
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DOI：
10.1016/0141-8130(94)90028-0
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发表时间：
1994-10-01
影响因子：
8.2
通讯作者：
LENTINI, A
中科院分区：
文献类型：
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作者：
GHOSH, P;HUTADILOK, N;LENTINI, A
在磷脂二棕榈酰-D,L-α-磷脂酰胆碱 (DPC) 存在和不存在的情况下，通过 H-1-NMR 光谱测定不同分子量的透明质酸 (HA) 溶液的链柔性。通过观察 HA 分子的乙酰胺脱氧葡萄糖残基的甲基质子的半峰线宽 (Delta v(1/2)) 可以确定，用 DPC 对高分子量或低分子量 HA 进行长达 120 分钟的超声处理可显着增加 HA 链的灵活性。纯化的高分子量 HA (Healon ) 与 H-3-DPC 或 H-3-血小板活化因子 (PAF) 的混合物的凝胶渗透色谱显示，在 HA 存在的情况下，这些放射性标记的分子会从凝胶中排除，但在 HA 不存在的情况下则不会。 Superose 6 层析后使用多角度激光光散射 (MALLS) 光度测定法对 DPC 和 Healon(R) 超声处理进行的研究表明，相对于不含 DPC 的 HA 对照超声处理，HA (M) 相对于 bar(w)、(M) 相对于 bar(n)、(M) 相对于 bar(z) 以及相应的均方根半径有所增加。从这些数据中，我们推断出 DPC 通过竞争 HA 链上的疏水中心来与 HA 结合，这些疏水中心通常负责链间和链内相互作用，并赋予 HA 分子刚性。有人提出，关节炎关节中的这种相互作用可以降低滑液粘弹性，从而削弱该介质保护关节软骨免受机械损伤的能力。
The chain flexibility of solutions of hyaluronan (HA) of different molecular weights was determined by H-1-NMR spectroscopy in the absence and presence of the phospholipid dipalmitoyl-D,L-alpha-phosphatidylcholine (DPC). Sonication of high- or low-molecular-weight HA with DPC for periods of up to 120 min markedly increased HA chain flexibility as determined by observing the half-peak linewidths (Delta v(1/2)) for the methyl protons of the acetamidodeoxyglucose residues of the HA molecules. Gel permeation chromatography of mixtures of purified high-molecular-weight HA (Healon(R)) with H-3-DPC or H-3-platelet activating factor (PAF) showed exclusion of these radioactively labelled molecules from the gel in the presence of HA but not in its absence. Studies using multi-angle laser-light-scattering (MALLS) photometry of sonicates of DPC and Healon(R) after Superose 6 chromatography revealed increases in HA (M) over bar(w), (M) over bar(n), (M) over bar(z),and their corresponding root mean square radii relative to control sonicates of HA without DPC. From these data, we have deduced that DPC binds to HA by competing for those hydrophobic centres along the HA chain which are normally responsible for the inter- and intra-chain interactions and which confer stiffness to the HA molecule. It is proposed that such interactions in arthritic joints could reduce synovial fluid viscoelasticity thereby diminishing the ability of this medium to protect articular cartilage from mechanical injury.