التفاصيل البيبلوغرافية
| العنوان: |
Re-Examining Interaction between Antimicrobial Peptide Aurein 1.2 and Model Cell Membranes via SFG |
| المؤلفون: |
Chu Wang (62506), Yong-Hao Ma (2869658), Xiaofeng Han (151229), Xiaolin Lu (293692) |
| سنة النشر: |
2022 |
| مصطلحات موضوعية: |
Biophysics, Biochemistry, Medicine, Cell Biology, Molecular Biology, Biotechnology, Virology, Computational Biology, Biological Sciences not elsewhere classified, Chemical Sciences not elsewhere classified, Physical Sciences not elsewhere classified, terminal phenylalanine residue, highly efficient 13, dependent signal intensity, c – h, residue antimicrobial peptide, aur molecules interact, aur molecules came, subsequent descending α, negatively charged lipids, interfacial interaction process, charged lipids, examining interaction, antimicrobial mechanism, adsorption process, aur ), sharp rise, necessary support, mechanism study, like aggregates |
| الوصف: |
Aurein 1.2 (Aur), a highly efficient 13-residue antimicrobial peptide (AMP) with a broad-spectrum antibiotic activity originally derived from the Australian frog skin secretions, can nonspecifically disrupt bacterial membranes. To deeply understand the molecular-level detail of the antimicrobial mechanism, here, we artificially established comparative experimental models to investigate the interfacial interaction process between Aur and negatively charged model cell membranes via sum frequency generation vibrational spectroscopy. Sequencing the vibrational signals of phenyl, C–H, and amide groups from Aur has characteristically helped us differentiate between the initial adsorption and subsequent insertion steps upon mutual interaction between Aur and the charged lipids. The phenyl group at the terminal phenylalanine residue can act as an anchor in the adsorption process. The time-dependent signal intensity of α-helices showed a sharp rise once the Aur molecules came into contact with the negatively charged lipids, indicating that the adsorption process was ongoing. Insertion of Aur into the charged lipids then offered the detectable interfacial C–H signals from Aur. The achiral and chiral amide I signals suggest that Aur had formed β-folding-like aggregates after interacting with the charged lipids, along with the subsequent descending α-helical amide I signals. The above-mentioned experimental results provide the molecular-level detail on how the Aur molecules interact with the cell membranes, and such a mechanism study can offer the necessary support for the AMP design and later application. |
| نوع الوثيقة: |
article in journal/newspaper |
| اللغة: |
unknown |
| العلاقة: |
https://figshare.com/articles/journal_contribution/Re-Examining_Interaction_between_Antimicrobial_Peptide_Aurein_1_2_and_Model_Cell_Membranes_via_SFG/21786922Test |
| DOI: |
10.1021/acs.langmuir.2c03068.s001 |
| الإتاحة: |
https://doi.org/10.1021/acs.langmuir.2c03068.s001Test |
| حقوق: |
CC BY-NC 4.0 |
| رقم الانضمام: |
edsbas.DC843535 |
| قاعدة البيانات: |
BASE |
