Time-resolved insertion of PB1−1 into a POPC bilayer (900-ns MD).

<p>Snapshots taken at 0, 500, and 900 ns illustrate the step-wise penetration of PB1−1 across the bilayer. In expanded insets, the arginines of PB1−1 form electrostatic as well as hydrogen-bonding contacts with lipid phosphohead groups, in effect securing the peptide. Together, these images su...

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Detalles Bibliográficos
Autor Principal:	Sanaz Sadeh (22813266) (author)
Outros autores:	Amir Ghaemi (15476466) (author), Nazila Arbab Soleimani (22813269) (author), Majid Moghbeli (22813272) (author), Golnaz BahramAli (22813275) (author)
Publicado:	2025
Subjects:	Biochemistry Medicine Cell Biology Pharmacology Biotechnology Immunology Space Science Environmental Sciences not elsewhere classified Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified sialic acid receptors purely computational scope molecular dynamics simulations mimetic entry pathways low predicted toxicity highly effective means direct membrane permeation assessed using mlcpp assessed using alphafold peptides take advantage require experimental validation pb1 &# 8722 integrating uptake efficiency designing influenza virus mediated lung targeting good safety profiles safety profiles mediated endocytosis penetrating peptides derived peptides suitable candidates successful vaccination study sought structural properties strong affinity stable complex respiratory therapy pointed towards physicochemical properties paramount importance nucleic acids including clathrin identified influenza drug compounds delivering antigens cpp candidates considered hypothesis antigen delivery
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Time-resolved insertion of PB1−1 into a POPC bilayer (900-ns MD).

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