Evidence map›Paper›PMID 19351165›Full record

ArticleThe journal of physical chemistry. B2009

Photoinduced unfolding of beta-lactoglobulin mediated by a water-soluble porphyrin.

John Belcher, Samuel Sansone, Nicholas F Fernandez, William E Haskins, Lorenzo Brancaleon, Lorenzo Brancaleona

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

9 citing papers in PubMed, 30 citations in OpenAlex.

  1. Organic-solvent mediated self-assembly of protoporphyrin IX with human serum albumin.International journal of biological macromolecules · 2025
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Effects of Visible-Light Irradiation of Protoporphyrin IX on the Self-Assembly of Tubulin Heterodimers.Chemphyschem : a European journal of chemical physics and physical chemistry · 2016
    Article
  8. Article
  9. Article
4 · The record

Corrections and comments

  • Erratum issued
    Brancaleona, Lorenzo [corrected to Brancaleon, Lorenzo]
5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

John BelcherDepartment of Physics and Astronomy, University of Texas at San Antonio, One UTSA Circle, San Antonio, Texas 78249, USA.
Samuel Sansone
Nicholas F Fernandez
William E Haskins
Lorenzo Brancaleon
Lorenzo Brancaleona
The University of Texas at San Antonio · US

Funding

STRUCTURAL VISUALIZATION IN BIOINFORMATICSG12RR013646 · NCRR · UNIVERSITY OF TEXAS SAN ANTONIO · PI WENK, CAROLA · 1998 to 2011
$19.6M
UTSA Maximizing Access to Research Careers Research Training Program - Admin SupplementT34GM007717 · NIGMS · UNIVERSITY OF TEXAS SAN ANTONIO · PI BAREA-RODRIGUEZ, EDWIN J · 1985 to 2021
$9.5M
NCRR NIH HHS G12 RR013646NIGMS NIH HHS GM07717NIGMS NIH HHS T34 GM007717
6 · The paper itself

Abstract

We investigated the effects that the irradiation of a tetra-anionic porphyrin (mesotetrakis(sulfonatophenyl)porphyrin) noncovalently bound to beta-lactoglobulin (BLG) produces on the conformation of the protein. Although BLG is not a potential target for the biomedical applications of porphyrins, it is a useful model for investigating the effects of photoactive ligands on small globular proteins. We show in this paper that irradiation causes a large unfolding of the protein and that the conformational change is not mediated by the formation of reactive oxygen species. Instead, our data are consistent with an electron-transfer mechanism that is capable of triggering structural changes in the protein and causes the Trp19 residue to undergo chemical modifications to form a derivative of kynurenine. This demonstrates that protein unfolding is prompted by a type-III photosensitizing mechanisms. Type-III mechanisms have been suggested previously, but they have been largely neglected as useful mediators of biomolecular damage. Our study demonstrates that porphyrins can be used as mediators of localized protein conformational changes and that the biomedical applications as well as the mechanistic details of electron transfer between exogenous ligands and proteins merit further investigation.

Indexed as

LasersCircular DichroismFluorescenceLactoglobulinsPhotochemistryPorphyrinsProtein FoldingSolubilityWaterLactoglobulinsmesotetrakis(sulfonatophenyl)porphyrinPorphyrinsWater

Identifiers

PMID19351165
PMCPMC2735475
OpenAlexW2046971384

What OpenQuestion holds

Textmetadata
LicenceTDM
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.