Evidence map›Paper›PMID 32194324›Full record

ArticleSaudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society2020

Molecular interaction of tea catechin with bovine β-lactoglobulin: A spectroscopic and in silico studies.

Nasser Abdulatif Al-Shabib, Javed Masood Khan, Ajamaluddin Malik, Md Tabish Rehman, Mohamed F AlAjmi, Fohad Mabood Husain, Malik Hisamuddin, Nojood Altwaijry

Open access · hybridAbstract read
In one paragraph

Article in Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

16 citing papers in PubMed, 95 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Study on the astringent mechanism ofFood chemistry: X · 2025
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Alpha-glucosidase inhibitors fromSaudi journal of biological sciences · 2022
    Article
  14. Article
  15. Article
  16. 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

8 authors at 2 institutions in 2 countries.

Nasser Abdulatif Al-ShabibDepartment of Food Science and Nutrition, Faculty of Food and Agricultural Sciences, King Saud University, 2460, Riyadh 11451, Saudi Arabia.
Javed Masood KhanDepartment of Food Science and Nutrition, Faculty of Food and Agricultural Sciences, King Saud University, 2460, Riyadh 11451, Saudi Arabia.
Ajamaluddin MalikProtein Research Chair, Department of Biochemistry, College of Science, King Saud University, Riyadh, Saudi Arabia.
Md Tabish RehmanKing Saud University, Department of Pharmacognosy, College of Pharmacy, Riyadh 11451, Saudi Arabia.
Mohamed F AlAjmiKing Saud University, Department of Pharmacognosy, College of Pharmacy, Riyadh 11451, Saudi Arabia.
Fohad Mabood HusainDepartment of Food Science and Nutrition, Faculty of Food and Agricultural Sciences, King Saud University, 2460, Riyadh 11451, Saudi Arabia.
Malik HisamuddinCentre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, India.
Nojood AltwaijryProtein Research Chair, Department of Biochemistry, College of Science, King Saud University, Riyadh, Saudi Arabia.
King Saud University · SAJamia Millia Islamia · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Polyphenols has attained pronounced attention due to their beneficial values of health and found to prevent several chronic diseases. Here, we elucidated binding mechanism between frequently consumed polyphenol "tea catechin" and milk protein bovine beta-lactoglobulin (β-Lg). We investigated the conformational changes of β-Lg due to interaction with catechin using spectroscopic and in silico studies. Fluorescence quenching data (Stern-Volmer quenching constant) revealed that β-Lg interacted with catechin via dynamic quenching. Thermodynamic data revealed that the interaction between β-Lg and catechin is endothermic and spontaneously interacted mainly through hydrophobic interactions. The UV-Vis absorption and far-UV circular dichroism (CD) spectroscopy exhibited that the tertiary as well as secondary structure of β-Lg distorted after interaction with catechin. Molecular docking and simulation studies also confirm that catechin binds at the central cavity of β-Lg with high affinity (~10

Indexed as

Beta-LactoglobulinCatechinPolyphenolProtein and proteinligand, interaction

Identifiers

PMID32194324
PMCPMC7078544
OpenAlexW3004091392

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.