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Effect of terminal arrangement of tryptophan on biological activity of symmetric α‐helix‐forming peptides.
- Published in:
- Chemical Biology & Drug Design, 2019, v. 94, n. 6, p. 2051, doi. 10.1111/cbdd.13608
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- Article
The C-terminal sequences of porcine thrombin are active as antimicrobial peptides.
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- Chemical Biology & Drug Design, 2016, v. 88, n. 6, p. 905, doi. 10.1111/cbdd.12824
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- Article
Symmetrical Modification of Minimized Dermaseptins to Extend the Spectrum of Antimicrobials with Endotoxin Neutralization Potency.
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- International Journal of Molecular Sciences, 2019, v. 20, n. 6, p. 1417, doi. 10.3390/ijms20061417
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- Article
Optimization of Antibacterial Activity in Tibetan Swine α-Helix Peptide TP by Site-Directed Mutagenesis.
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- Frontiers in Microbiology, 2022, v. 13, p. 1, doi. 10.3389/fmicb.2022.864374
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- Article
Antimicrobial Peptides: Cross‐Strand Interaction, Central Bending, and Sequence Pattern Act as Biomodulators of Simplified β‐Hairpin Antimicrobial Amphiphiles (Small 7/2021).
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- Small, 2021, v. 17, n. 7, p. 1, doi. 10.1002/smll.202170029
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- Article
Cross‐Strand Interaction, Central Bending, and Sequence Pattern Act as Biomodulators of Simplified β‐Hairpin Antimicrobial Amphiphiles.
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- Small, 2021, v. 17, n. 7, p. 1, doi. 10.1002/smll.202003899
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- Article
Expression of T9W in Pichia pastoris and the protective roles of T9W in ICR Mice.
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- Biotechnology Letters, 2020, v. 42, n. 1, p. 67, doi. 10.1007/s10529-019-02759-2
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- Article
Antimicrobial activity and membrane-active mechanism of tryptophan zipper-like β-hairpin antimicrobial peptides.
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- Amino Acids, 2015, v. 47, n. 11, p. 2385, doi. 10.1007/s00726-015-2029-7
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- Article