ArticleAntibiotics (Basel, Switzerland)2023
Evidence of Self-Association and Conformational Change in Nisin Antimicrobial Polypeptide Solutions: A Combined Raman and Ultrasonic Relaxation Spectroscopic and Theoretical Study.
Article in Antibiotics (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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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.
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Who cites it
4 citing papers in PubMed, 13 citations in OpenAlex.
- Apoptotic and anti-inflammatory effect of nisin-loaded sodium alginate-gum arabic nanoparticles against colon cancer cells.International journal of biological macromolecules · 2025Article
- Kinetic and Structural Insights into β-Cyclodextrin Complexation with Asparagine Enantiomers: An Experimental and Theoretical Study.Molecules (Basel, Switzerland) · 2025Article
- Nisin and ε-polylysine combined treatment enhances quality of fresh-cut jackfruit at refrigerated storage.Frontiers in nutrition · 2024Article
- Identification of Aggregation Processes in Hexamethylenetetramine Aqueous Solutions: A Comprehensive Raman and Acoustic Spectroscopic Study Combined with Density Functional Theory Calculations.Molecules (Basel, Switzerland) · 2023Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The polypeptide Nisin is characterized by antibacterial properties, making it a compound with many applications, mainly in the food industry. As a result, a deeper understanding of its behaviour, especially after its dissolution in water, is of the utmost importance. This could be possible through the study of aqueous solutions of Nisin by combining vibrational and acoustic spectroscopic techniques. The velocity and attenuation of ultrasonic waves propagating in aqueous solutions of the polypeptide Nisin were measured as a function of concentration and temperature. The computational investigation of the molecular docking between Nisin monomeric units revealed the formation of dimeric units. The main chemical changes occurring in Nisin structure in the aqueous environment were tracked using Raman spectroscopy, and special spectral markers were used to establish the underlying structural mechanism. Spectral changes evidenced the presence of the dimerization reaction between Nisin monomeric species. The UV/Vis absorption spectra were dominated by the presence of π → π* transitions in the peptide bonds attributed to secondary structural elements such as α-helix, β-sheets and random coils. The analysis of the acoustic spectra revealed that the processes primarily responsible for the observed chemical relaxations are probably the conformational change between possible conformers of Nisin and its self-aggregation mechanism, namely, the dimerization reaction. The activation enthalpy and the enthalpy difference between the two isomeric forms were estimated to be equal to
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Registered trials
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.