Disulfide engineering on temporin-SHf: Stabilizing the bioactive conformation of an ultra-short antimicrobial peptide.
Amino Acid Sequence
Anti-Bacterial Agents
/ chemistry
Antimicrobial Cationic Peptides
/ chemistry
Disulfides
/ chemistry
Drug Design
Hydrogen-Ion Concentration
Hydrophobic and Hydrophilic Interactions
Microbial Sensitivity Tests
Models, Molecular
Molecular Conformation
Peptides
/ chemistry
Protein Binding
Protein Denaturation
Proteolysis
NMR spectroscopy
antimicrobial peptide
cysteine disulfide
proteolysis
temporin-SHf
Journal
Chemical biology & drug design
ISSN: 1747-0285
Titre abrégé: Chem Biol Drug Des
Pays: England
ID NLM: 101262549
Informations de publication
Date de publication:
09 2019
09 2019
Historique:
received:
12
09
2018
revised:
07
03
2019
accepted:
17
03
2019
pubmed:
30
3
2019
medline:
17
9
2020
entrez:
30
3
2019
Statut:
ppublish
Résumé
In Silico searching for short antimicrobial peptides has revealed temporin-SHf as the short (8AA), hydrophobic, broad spectrum, and natural antimicrobial peptide. Important drawback associated with temporin-SHf is the susceptibility of its bioactive conformation for denaturation and proteolytic degradation. In the current report, disulfide engineering strategy has been adopted to improve the stability of bioactive conformation of temporin-SHf. The functionally non-critical Leu4 and Ile7 residues at i and i + 3 position of helical conformation of temporin-SHf were mutated with cysteine disulfide. Designed [L4C, I7C]temporin-SHf was synthesized, characterized using NMR spectroscopy, and accessed for antimicrobial activity. [L4C, I7C]Temporin-SHf adopts helical conformation from Phe3 to Phe8 in the absence of membrane-mimetic environment and retains broad spectrum antimicrobial activity. The reduction potential of cysteine disulfide of [L4C, I7C]temporin-SHf is -289 mV. Trypsin-induced digestion and serum-induced digestion have confirmed the advantage of cysteine disulfide in imparting proteolytic stability to temporin-SHf. Disulfide-stabilized temporin-SHf may serve as a good model for the rational design of temporin-SHf based antibiotics for treatment of infectious diseases.
Substances chimiques
Anti-Bacterial Agents
0
Antimicrobial Cationic Peptides
0
Disulfides
0
Peptides
0
temporin
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1634-1646Informations de copyright
© 2019 John Wiley & Sons A/S.
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