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通过近红外光谱理解透明质酸诱导的水结构变化。

Understanding hyaluronic acid induced variation of water structure by near-infrared spectroscopy.

机构信息

School of Pharmaceutical Sciences, Shandong University, Wenhuaxi Road 44, Jinan, 250012, China.

Bloomage Biotechnology Corporation Limited, Tianchen Street 678, Jinan, 250012, China.

出版信息

Sci Rep. 2020 Jan 28;10(1):1387. doi: 10.1038/s41598-020-58417-5.

DOI:10.1038/s41598-020-58417-5
PMID:31992833
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6987104/
Abstract

In order to understand the hydration effect of hyaluronic acid (HA) in aqueous solution, near-infrared (NIR) spectroscopy was used to investigate the HA aqueous solutions at different concentrations and temperature. As HA concentration was raised, there was a nonlinear change in absorption value in the first overtone region of OH, indicating the changes of hydration water. A reconstructed spectrum based on principal component analysis (PCA) was established and analyzed with the concept of aquaphotomics. The results showed that HA acted as a structure maker to make water molecules arranged in order. Water species with two hydrogen bonds (S) and three hydrogen bonds (S) showed the decrease at low concentration range of 0-40 mg/mL, but increased at higher concentration, indicating the difference in water species at different HA concentration. Meanwhile, HA had the ability to improve the thermal stability of water structure, suggesting a potential bio-protective function. This study provides a unique perspective on the molecular interactions between HA and water molecules, which is helpful for understanding the role of HA in life process and may serve as the basis for HA applications.

摘要

为了理解透明质酸(HA)在水溶液中的水合作用,本研究采用近红外(NIR)光谱法研究了不同浓度和温度下的 HA 水溶液。随着 HA 浓度的升高,OH 基第一泛频区的吸收值呈非线性变化,表明水合水发生了变化。基于主成分分析(PCA)建立了重建光谱,并用水质组学的概念进行了分析。结果表明,HA 作为结构形成剂使水分子有序排列。具有两个氢键(S)和三个氢键(S)的水分子在 0-40mg/mL 的低浓度范围内减少,但在较高浓度下增加,表明不同 HA 浓度下水分子的种类不同。同时,HA 具有提高水结构热稳定性的能力,表明其具有潜在的生物保护功能。本研究为 HA 与水分子之间的分子相互作用提供了独特的视角,有助于理解 HA 在生命过程中的作用,并可能为 HA 的应用提供基础。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd28/6987104/b9e78896bb8f/41598_2020_58417_Fig8_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd28/6987104/51ae2667fab8/41598_2020_58417_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd28/6987104/52f4dbbe1148/41598_2020_58417_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd28/6987104/fbadc01fd81a/41598_2020_58417_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd28/6987104/f07ff7a5b44e/41598_2020_58417_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd28/6987104/73d2804e2aac/41598_2020_58417_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd28/6987104/b926d885d249/41598_2020_58417_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd28/6987104/0e61781007c2/41598_2020_58417_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd28/6987104/b9e78896bb8f/41598_2020_58417_Fig8_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd28/6987104/51ae2667fab8/41598_2020_58417_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd28/6987104/52f4dbbe1148/41598_2020_58417_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd28/6987104/fbadc01fd81a/41598_2020_58417_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd28/6987104/f07ff7a5b44e/41598_2020_58417_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd28/6987104/73d2804e2aac/41598_2020_58417_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd28/6987104/b926d885d249/41598_2020_58417_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd28/6987104/0e61781007c2/41598_2020_58417_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd28/6987104/b9e78896bb8f/41598_2020_58417_Fig8_HTML.jpg

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