Design of a novel tryptophan-rich membrane-active antimicrobial peptide from the membrane-proximal region of the HIV glycoprotein, gp41

Scholarly Works

• Akhash, N.; Farajzadeh Sheikh, A.; Farshadzadeh, Z. Design of a novel analogue peptide with potent antibiofilm activities against Staphylococcus aureus based upon a sapecin B-derived peptide. Scientific reports 2024, 14, 2256. doi:10.1038/s41598-024-52721-0
• Straus, S. K. Tryptophan- and arginine-rich antimicrobial peptides: Anti-infectives with great potential. Biochimica et biophysica acta. Biomembranes 2023, 1866, 184260. doi:10.1016/j.bbamem.2023.184260
• Mumtaz, S.; Behera, S.; Joshi, S.; Mukhopadhyay, K. Efficacy and Toxicity Studies of Novel α-MSH Analogues with Antibiofilm Action and β-Lactam Resensitization Potential against MRSA. ACS infectious diseases 2022, 8, 2480–2493. doi:10.1021/acsinfecdis.2c00280
• Wei, J.; Cao, X.; Qian, J.; Liu, Z.; Wang, X.; Su, Q.; Wang, Y.; Xie, R.; Li, X. Evaluation of antimicrobial peptide LL-37 for treatment of Staphylococcus aureus biofilm on titanium plate. Medicine 2021, 100, e27426. doi:10.1097/md.0000000000027426
• Drayton, M.; Deisinger, J. P.; Ludwig, K. C.; Raheem, N.; Müller, A.; Schneider, T.; Straus, S. K. Host Defense Peptides: Dual Antimicrobial and Immunomodulatory Action. International journal of molecular sciences 2021, 22, 11172. doi:10.3390/ijms222011172
• Sahoo, A.; Swain, S. S.; Behera, A.; Sahoo, G.; Mahapatra, P. K.; Panda, S. K. Antimicrobial Peptides Derived From Insects Offer a Novel Therapeutic Option to Combat Biofilm: A Review. Frontiers in microbiology 2021, 12, 661195. doi:10.3389/fmicb.2021.661195
• Rounds, T.; Straus, S. K. Lipidation of Antimicrobial Peptides as a Design Strategy for Future Alternatives to Antibiotics. International journal of molecular sciences 2020, 21, 9692. doi:10.3390/ijms21249692
• Lee, H.; Yang, S.-T.; Shin, S. Y. Improved Cell Selectivity of Symmetric α‐Helical Peptides Derived From Trp‐Rich Antimicrobial Peptides. Bulletin of the Korean Chemical Society 2020, 41, 930–936. doi:10.1002/bkcs.12091
• Bhattacharjya, S.; Straus, S. K. Design, Engineering and Discovery of Novel α-Helical and β-Boomerang Antimicrobial Peptides against Drug Resistant Bacteria. International journal of molecular sciences 2020, 21, 5773. doi:10.3390/ijms21165773
• Raheem, N.; Kumar, P.; Lee, E.; Cheng, J. T.; Hancock, R. E. W.; Straus, S. K. Insights into the mechanism of action of two analogues of aurein 2.2. Biochimica et biophysica acta. Biomembranes 2020, 1862, 183262. doi:10.1016/j.bbamem.2020.183262
• Raheem, N.; Straus, S. K. Mechanisms of Action for Antimicrobial Peptides With Antibacterial and Antibiofilm Functions. Frontiers in microbiology 2019, 10, 2866. doi:10.3389/fmicb.2019.02866
• Dal Mas, C.; Pinheiro, D.; Campeiro, J. D.; Mattei, B.; Oliveira, V.; Oliveira, E. B.; Miranda, A.; Perez, K. R.; Hayashi, M. A. F. Biophysical and biological properties of small linear peptides derived from crotamine, a cationic antimicrobial/antitumoral toxin with cell penetrating and cargo delivery abilities. Biochimica et biophysica acta. Biomembranes 2017, 1859, 2340–2349. doi:10.1016/j.bbamem.2017.09.006
• Hasek, M. L.; Steckbeck, J. D.; Deslouches, B.; Craigo, J. K.; Montelaro, R. C. Engineered Cationic Antimicrobial Peptides Containing Cholesterol InteractingMotifs to Target Viral Envelopes. Journal of Antivirals & Antiretrovirals 2017, 9, 18–31. doi:10.4172/1948-5964.1000158
• Haney, E. F.; Mansour, S. C.; Hancock, R. E. W. Antimicrobial Peptides: An Introduction. Methods in molecular biology (Clifton, N.J.) 2016, 1548, 3–22. doi:10.1007/978-1-4939-6737-7_1
• Palmieri, G.; Balestrieri, M.; Proroga, Y. T. R.; Falcigno, L.; Facchiano, A.; Riccio, A.; Capuano, F.; Marrone, R.; Neglia, G.; Anastasio, A. New antimicrobial peptides against foodborne pathogens: From in silico design to experimental evidence. Food chemistry 2016, 211, 546–554. doi:10.1016/j.foodchem.2016.05.100
• Su, T.; Yang, H.; Fan, Q.; Jia, D.; Tao, Z.; Wan, L.; Lu, X. Enhancing the circulating half-life and the antitumor effects of a tumor-selective cytotoxic peptide by exploiting endogenous serum albumin as a drug carrier. International journal of pharmaceutics 2016, 499, 195–204. doi:10.1016/j.ijpharm.2015.12.069
• Jittikoon, J.; Ngamsaithong, N.; Pimthon, J.; Vajragupta, O. Effect of N-terminal truncation on antibacterial activity, cytotoxicity and membrane perturbation activity of Cc-CATH3. Archives of pharmacal research 2015, 38, 1839–1849. doi:10.1007/s12272-015-0600-0
• Arias, M.; Nguyen, L. T.; Kuczynski, A. M.; Lejon, T.; Vogel, H. J. Position-Dependent Influence of the Three Trp Residues on the Membrane Activity of the Antimicrobial Peptide, Tritrpticin. Antibiotics (Basel, Switzerland) 2014, 3, 595–616. doi:10.3390/antibiotics3040595
• Wood, S. J.; Park, Y. A.; Kanneganti, N. P.; Mukkisa, H. R.; Crisman, L. L.; Davis, S. E.; Vandenbosch, J. L.; Scaglione, J. B.; Heyl, D. L. Modified cysteine-deleted tachyplesin (CDT) analogs as linear antimicrobial peptides: Influence of chain length, positive charge, and hydrophobicity on antimicrobial and hemolytic activity. International Journal of Peptide Research and Therapeutics 2014, 20, 519–530. doi:10.1007/s10989-014-9419-7
• Koller, D.; Lohner, K. The role of spontaneous lipid curvature in the interaction of interfacially active peptides with membranes. Biochimica et biophysica acta 2014, 1838, 2250–2259. doi:10.1016/j.bbamem.2014.05.013

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