Evidence map›Paper›PMID 28644391›Full record

ArticleMolecules (Basel, Switzerland)2017

Molecular Structure-Affinity Relationship of Flavonoids in Lotus Leaf (Nelumbo nucifera Gaertn.) on Binding to Human Serum Albumin and Bovine Serum Albumin by Spectroscopic Method.

Xiaosheng Tang, Ping Tang, Liangliang Liu

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.1field-weighted citation impact, top 23% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Phytochemicals and Immunomodulatory Effect ofPlants (Basel, Switzerland) · 2021
    Article
  7. Article
  8. Hydrophobics of CRSC advances · 2019
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 3 institutions in 1 country.

Xiaosheng TangHubei Key Laboratory of Edible Wild Plants Conservation and Utilization & National Demonstration Center for Experimental Biology Education & College of Life Sciences, Hubei Key Laboratory of Pollutant Analysis & Reuse Technology, Hubei Normal University, Huangshi 435002, China. xiaoshengtang@yahoo.com.
Ping TangInstitute of Bast Fiber Crops, Chinese Academy of Agricultural Sciences, Changsha 410205, China. pingtang@yahoo.com.
Liangliang LiuInstitute of Bast Fiber Crops, Chinese Academy of Agricultural Sciences, Changsha 410205, China. liuliangliang@caas.cn.
Chinese Academy of Agricultural Sciences · CNHubei Normal University · CNInstitute of Bast Fiber Crops · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lotus leaf has gained growing popularity as an ingredient in herbal formulations due to its various activities. As main functional components of lotus leaf, the difference in structure of flavonoids affected their binding properties and activities. In this paper, the existence of 11 flavonoids in lotus leaf extract was confirmed by High Performance Liquid Chromatography (HPLC) analysis and 11 flavonoids showed various contents in lotus leaf. The interactions between lotus leaf extract and two kinds of serum albumins (human serum albumin (HSA) and bovine serum albumin (BSA)) were investigated by spectroscopic methods. Based on the fluorescence quenching, the interactions between these flavonoids and serum albumins were further checked in detail. The relationship between the molecular properties of flavonoids and their affinities for serum albumins were analyzed and compared. The hydroxylation on 3 and 3' position increased the affinities for serum albumins. Moreover, both of the methylation on 3' position of quercetin and the C₂=C₃ double bond of apigenin and quercetin decreased the affinities for HSA and BSA. The glycosylation lowered the affinities for HSA and BSA depending on the type of sugar moiety. It revealed that the hydrogen bond force played an important role in binding flavonoids to HSA and BSA.

Indexed as

AnimalsCattleChromatography, High Pressure LiquidFlavonoidsHumansHydroxylationNelumboPlant LeavesProtein BindingSerum AlbuminSpectrometry, FluorescenceStructure-Activity RelationshipFlavonoidsSerum Albuminbovine serum albuminflavonoidsfluorescence spectroscopyhuman serum albumininteractionlotus leaf

Identifiers

PMID28644391
PMCPMC6152052
OpenAlexW2633497416

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.