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Coordination pattern and reactivity of two model peptides from porin protein P1
- Source :
- Journal of inorganic biochemistry. 215
- Publication Year :
- 2020
-
Abstract
- It has been reported that numerous of Fusobacterium nucleatum outer membrane proteins take part in cancerogenesis. Therefore, it is very interesting to study their interactions with metal ions and the ability to produce reactive oxygen species, which may be involved in cancer progression. Since investigations of metal binding to proteins are often based on fragments that contain the metal-binding domains, designing model peptides should be very mindful. As was shown in this paper, very similar protein fragments may behave differentially. Herein, combined potentiometric, spectroscopic, and computational studies were performed to determine metal ion binding by ligands constituting fragments of porin protein P1. Two studied tetrapeptides (Ac-KEHK-NH2 and Ac-EHKA-NH2) that have common EHK motif have different coordination properties and reactivity. Therefore, we should be cautious when transferring the behavior of small peptide fragments to whole protein.
- Subjects :
- Metal ions in aqueous solution
Potentiometric titration
Porins
010402 general chemistry
Ligands
01 natural sciences
Biochemistry
Inorganic Chemistry
Metal
Coordination Complexes
Neoplasms
Protein P1
DNA Cleavage
chemistry.chemical_classification
Reactive oxygen species
biology
Fusobacterium nucleatum
010405 organic chemistry
Chemistry
Circular Dichroism
Hydrogen Peroxide
biology.organism_classification
Peptide Fragments
0104 chemical sciences
visual_art
Porin
visual_art.visual_art_medium
Potentiometry
Bacterial outer membrane
Peptides
Reactive Oxygen Species
Copper
Bacterial Outer Membrane Proteins
Subjects
Details
- ISSN :
- 18733344
- Volume :
- 215
- Database :
- OpenAIRE
- Journal :
- Journal of inorganic biochemistry
- Accession number :
- edsair.doi.dedup.....954b0413b7e9cdc36cdd57a5a26f9773