The Expression of Antibacterial Peptide Turgencin A in
Pichia pastoris
Staphylococcus aureus
antimicrobial peptide
membrane damage
pork preservation
Journal
Molecules (Basel, Switzerland)
ISSN: 1420-3049
Titre abrégé: Molecules
Pays: Switzerland
ID NLM: 100964009
Informations de publication
Date de publication:
14 Jul 2023
14 Jul 2023
Historique:
received:
07
06
2023
revised:
04
07
2023
accepted:
11
07
2023
medline:
31
7
2023
pubmed:
29
7
2023
entrez:
29
7
2023
Statut:
epublish
Résumé
Antibiotic resistance to pathogenic bacteria is becoming an increasing public health threat, and identifying alternatives to antibiotics would be an effective solution to the problem of drug resistance. Antimicrobial peptides are small peptides produced by various organisms; they are considered to be adequate antibiotic substitutes because they have intense, broad-spectrum antibacterial activity and stability, are widely available, and target strains do not quickly develop resistance. Recent research on antimicrobial peptides has shown that they have broad potential for applications in medicine, agriculture, food, and animal feed. Turgencin A is a potent antimicrobial peptide isolated from the Arctic sea squirt. We established a His-tagged expression system for
Identifiants
pubmed: 37513276
pii: molecules28145405
doi: 10.3390/molecules28145405
pmc: PMC10384874
pii:
doi:
Substances chimiques
turgencin A
0
Anti-Bacterial Agents
0
Antimicrobial Cationic Peptides
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : National Natural Science Foundation of China
ID : 31900861
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