Evidence map›Paper›PMID 40488009›Full record

ArticleACS omega2025

Nanoliposomal Encapsulation and Purification of Angiotensin-Converting Enzyme Inhibitor Peptides from Ulva rigida.

Eda Şensu, Harun Koku, Evren Demircan, Sebahat Şişman, İbrahim Gülseren, Tuğçe Karaduman, Bilal Çakır, Emine Şükran Okudan, Gökhan Duruksu, Beraat Özçelik and 1 more

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Article in ACS omega, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing papers in PubMed
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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

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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

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0 citing papers in PubMed.

No citing paper in PubMed yet.

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

11 authors.

Eda ŞensuDepartment of Food Engineering, Faculty of Chemical and Metallurgical Engineering, Istanbul Technical University, Maslak, TR-34469 Istanbul, Türkiye.
Harun KokuDepartment of Chemical Engineering, Faculty of Engineering, Middle East Technical University, Dumlupınar Bulv. No. 1, 06800 Ankara, Türkiye.
Evren DemircanDepartment of Food Engineering, Faculty of Chemical and Metallurgical Engineering, Istanbul Technical University, Maslak, TR-34469 Istanbul, Türkiye.
Sebahat ŞişmanDepartment of Food Engineering, Istanbul Sabahattin Zaim University, Halkalı-Kuçukcekmece, 34303 Istanbul, Türkiye.
İbrahim GülserenDepartment of Food Engineering, Istanbul Sabahattin Zaim University, Halkalı-Kuçukcekmece, 34303 Istanbul, Türkiye.ORCID https://orcid.org/0000-0002-7339-1159
Tuğçe KaradumanDepartment of Molecular Biology and Genetics, Faculty of Science and Letters, Aksaray University, TR-68100 Aksaray, Türkiye.
Bilal ÇakırDepartment of Food Engineering, Istanbul Sabahattin Zaim University, Halkalı-Kuçukcekmece, 34303 Istanbul, Türkiye.
Emine Şükran OkudanFaculty of Fisheries, Akdeniz University, Dumlupınar Bulvarı, 07058 Antalya, Türkiye.
Gökhan DuruksuStem Cell and Gene Therapy Research and Applied Center, Kocaeli University, 41380 Kocaeli, Türkiye.ORCID https://orcid.org/0000-0002-3830-2384
Beraat ÖzçelikDepartment of Food Engineering, Faculty of Chemical and Metallurgical Engineering, Istanbul Technical University, Maslak, TR-34469 Istanbul, Türkiye.ORCID https://orcid.org/0000-0002-1810-8154
Aysun YücetepeDepartment of Food Engineering, Faculty of Engineering, Aksaray University, TR-68100 Aksaray, Türkiye.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Angiotensin-converting enzyme inhibitory peptides derived from natural sources may be effective in the treatment of hypertension without causing side effects compared with existing angiotensin-converting enzyme (ACE) inhibitors. Naturally derived antihypertensive peptides are therefore considered a promising alternative for the prevention or treatment of hypertension. Therefore, the study aimed to purify and identify ACE-inhibitory peptides from the green macroalgae Ulva rigida. In addition, the encapsulation of the purified peptides showed the highest ACE-inhibitory activity by chitosan-coated nanoliposomes, and the characterization of nanoliposomes was evaluated. Protein hydrolysates were obtained from U. rigida through enzymatic hydrolysis. The hydrolysates were separated into molecular weights of <3, <5, and <10 kDa through ultrafiltration membrane separation (UFMS). The <3 kDa fraction (UFMS-3) that exhibited the highest ACE-inhibitory activity (77.02%, 1 mg/mL) was purified using ion-exchange chromatography. Fraction-1 (IEC-F1) obtained from the ion-exchange purification showed an impressive 82.03% ACE-inhibitory activity. Moreover, peptide sequences of IEC-F1 were identified by LC-MS/MS, and their bioactive properties were determined

Identifiers

PMID40488009
PMCPMC12138630

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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.