Study on the self-assembly of aromatic antimicrobial peptides based on different PAF26 peptide sequences
Antimicrobial peptide (AMP) self-assembly is an effective way to synthesis antimicrobial biomaterials. In previous studies, we found PAF26 AMP (Ac-RKKWFW-NH2) and its derivative K2–F2 peptide (Ac-KKRKKWFWFF-NH2) could both self-assemble into hydrogels, but they had distinct microscopic structures. T...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
De Gruyter
2022-03-01
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| Series: | e-Polymers |
| Subjects: | |
| Online Access: | https://doi.org/10.1515/epoly-2022-0012 |
| _version_ | 1828108533417115648 |
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| author | Cao Fengyi Zhu Genxing Song Meng Zhao Xiaoli Ma Gangqing Zhang Mengqing |
| author_facet | Cao Fengyi Zhu Genxing Song Meng Zhao Xiaoli Ma Gangqing Zhang Mengqing |
| author_sort | Cao Fengyi |
| collection | DOAJ |
| description | Antimicrobial peptide (AMP) self-assembly is an effective way to synthesis antimicrobial biomaterials. In previous studies, we found PAF26 AMP (Ac-RKKWFW-NH2) and its derivative K2–F2 peptide (Ac-KKRKKWFWFF-NH2) could both self-assemble into hydrogels, but they had distinct microscopic structures. Therefore, in this work five PAF26 peptide derivatives with different numbers of aromatic amino acids are designed to better understand the self-assembly mechanism of aromatic AMP. The transmission electron microscopy, infrared spectroscopy, circular dichroism, and fluorescence spectroscopy characterizations are carried out to study the microscope structure, secondary conformation, and molecular interactions. It is found that the five peptide derivatives have different microscopic structures, and the number of aromatic amino acids will affect the peptide hydrogen bonding and aromatic stacking interactions, causing significant differences in the secondary conformation and microscopic structure. This work will enhance the comprehension of aromatic AMP self-assembly. |
| first_indexed | 2024-04-11T10:48:20Z |
| format | Article |
| id | doaj.art-f5b527b7831a4e70bead32d23cc5ad52 |
| institution | Directory Open Access Journal |
| issn | 1618-7229 |
| language | English |
| last_indexed | 2024-04-11T10:48:20Z |
| publishDate | 2022-03-01 |
| publisher | De Gruyter |
| record_format | Article |
| series | e-Polymers |
| spelling | doaj.art-f5b527b7831a4e70bead32d23cc5ad522022-12-22T04:28:59ZengDe Gruytere-Polymers1618-72292022-03-0122127628410.1515/epoly-2022-0012Study on the self-assembly of aromatic antimicrobial peptides based on different PAF26 peptide sequencesCao Fengyi0Zhu Genxing1Song Meng2Zhao Xiaoli3Ma Gangqing4Zhang Mengqing5School of Materials and Chemical Engineering, Zhongyuan University of Technology, Zhengzhou, 450007, ChinaSchool of Materials and Chemical Engineering, Zhongyuan University of Technology, Zhengzhou, 450007, ChinaSchool of Materials and Chemical Engineering, Zhongyuan University of Technology, Zhengzhou, 450007, ChinaSchool of Materials and Chemical Engineering, Zhongyuan University of Technology, Zhengzhou, 450007, ChinaSchool of Materials and Chemical Engineering, Zhongyuan University of Technology, Zhengzhou, 450007, ChinaSchool of Materials and Chemical Engineering, Zhongyuan University of Technology, Zhengzhou, 450007, ChinaAntimicrobial peptide (AMP) self-assembly is an effective way to synthesis antimicrobial biomaterials. In previous studies, we found PAF26 AMP (Ac-RKKWFW-NH2) and its derivative K2–F2 peptide (Ac-KKRKKWFWFF-NH2) could both self-assemble into hydrogels, but they had distinct microscopic structures. Therefore, in this work five PAF26 peptide derivatives with different numbers of aromatic amino acids are designed to better understand the self-assembly mechanism of aromatic AMP. The transmission electron microscopy, infrared spectroscopy, circular dichroism, and fluorescence spectroscopy characterizations are carried out to study the microscope structure, secondary conformation, and molecular interactions. It is found that the five peptide derivatives have different microscopic structures, and the number of aromatic amino acids will affect the peptide hydrogen bonding and aromatic stacking interactions, causing significant differences in the secondary conformation and microscopic structure. This work will enhance the comprehension of aromatic AMP self-assembly.https://doi.org/10.1515/epoly-2022-0012antimicrobial peptideself-assemblymicroscopic structuresecondary conformationmolecular interaction |
| spellingShingle | Cao Fengyi Zhu Genxing Song Meng Zhao Xiaoli Ma Gangqing Zhang Mengqing Study on the self-assembly of aromatic antimicrobial peptides based on different PAF26 peptide sequences e-Polymers antimicrobial peptide self-assembly microscopic structure secondary conformation molecular interaction |
| title | Study on the self-assembly of aromatic antimicrobial peptides based on different PAF26 peptide sequences |
| title_full | Study on the self-assembly of aromatic antimicrobial peptides based on different PAF26 peptide sequences |
| title_fullStr | Study on the self-assembly of aromatic antimicrobial peptides based on different PAF26 peptide sequences |
| title_full_unstemmed | Study on the self-assembly of aromatic antimicrobial peptides based on different PAF26 peptide sequences |
| title_short | Study on the self-assembly of aromatic antimicrobial peptides based on different PAF26 peptide sequences |
| title_sort | study on the self assembly of aromatic antimicrobial peptides based on different paf26 peptide sequences |
| topic | antimicrobial peptide self-assembly microscopic structure secondary conformation molecular interaction |
| url | https://doi.org/10.1515/epoly-2022-0012 |
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