Majid, Abdul and Naz, Farah and Jamro, Hatim Ali and Lal, Sham and Soomro, Inayatullah and Abbasi, Sanaullah and Ujjan, Safdar Ali (2021) Folding Behaviour and Antibacterial Activity of Ionic Complementary Peptide EAK-16. Journal of Pharmaceutical Research International, 33 (28A). pp. 122-130. ISSN 2456-9119
![[thumbnail of 2349-Article Text-4008-1-10-20221006.pdf]](http://info.submit4journal.com/style/images/fileicons/text.png)
2349-Article Text-4008-1-10-20221006.pdf - Published Version
Download (764kB)
Abstract
Aim: A major challenge in the development of new antibiotics is the biocompatibility within biological environment. Ionic complementary peptide (EAK-16) from amyloid protein, have the ability to adopt secondary structure conformation at membrane interfaces. This study aimed to investigate the effect of membrane on EAK-16 peptide folding and their antibacterial applications.
Methodology: We studied secondary structural conformation of EAK-16 using circular dichroism (CD) spectroscopy in an aqueous environment and at membrane bilayers interfaces. Initially, the antibacterial efficacy was investigated against both Gram-positive and Gram-negative bacteria. Membrane mimicking models were synthesised with dimyristoylphosphatidylcholine (DMPC) and dimyristoylphosphatidylserine (DMPS) lipid vesicles using calcein leakage assay.
Results: EAK-16 showed transition in secondary structural conformation. In aqueous environment, it was predominantly β-sheets and at membrane interfaces, it was mainly α-helical. EAK-16 peptide was highly active against bacteria (at minimum concentration applied) and membrane leakage was found to be > 60%. This effect was confirmed with both anionic lipids (DMPS) and neutral lipids (DMPC). The helical transition of EAK-16 could be a major factor to disrupt the membrane and bacterial death
Conclusion: The secondary structural conformation and calcein leakage data suggest that EAK-16 has potential to kill bacteria by adopting helical tilted conformation and membrane perturbation via lysis. This study revealed structure-function relationship of peptide and lipid bilayers to further investigate the mode of pore formation and mode of action of EAK-16 in membrane perturbation and antibacterial efficacy.
Item Type: | Article |
---|---|
Subjects: | Eurolib Press > Medical Science |
Depositing User: | Managing Editor |
Date Deposited: | 03 Mar 2023 06:20 |
Last Modified: | 02 Mar 2024 04:25 |
URI: | http://info.submit4journal.com/id/eprint/334 |