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Ultrashort Peptide Grafting on Mesoporous Films and Its Impact on Ionic Mesopore Accessibility

Bagherabadi, Mohadeseh ; Andrieu-Brunsen, Annette (2025)
Ultrashort Peptide Grafting on Mesoporous Films and Its Impact on Ionic Mesopore Accessibility.
In: Langmuir, 2024, 40 (8)
doi: 10.26083/tuprints-00026753
Artikel, Zweitveröffentlichung, Postprint

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Kurzbeschreibung (Abstract)

An approach for direct in-pore solid-phase ultrashort peptide synthesis on mesoporous films using the amino acids arginine, leucine, and glycine is presented. Although the number of grafted amino acids remains low, the ionic mesopore accessibility can be gradually adjusted. The addition of arginine in up to five reaction cycles leads to a progressive increase in positive mesopore charge density, which gradually increases the anionic mesopore accessibility at acidic pH. At basic pH, the remaining silanol groups at the pore wall still dominate counter-charged cation mesopore accessibility. Thus, specific peptide sequence design is demonstrated to be a sensitive tool for molecular transport control in nanoscale pores. Overall, the direct in-pore solid-phase ultrashort peptide synthesis on mesoporous films using the sequences of different amino acids opens up exciting opportunities for the development of innovative materials with precisely tailored properties and functions based on specific peptide sequence design.

Typ des Eintrags: Artikel
Erschienen: 2025
Autor(en): Bagherabadi, Mohadeseh ; Andrieu-Brunsen, Annette
Art des Eintrags: Zweitveröffentlichung
Titel: Ultrashort Peptide Grafting on Mesoporous Films and Its Impact on Ionic Mesopore Accessibility
Sprache: Englisch
Publikationsjahr: 13 Februar 2025
Ort: Darmstadt
Publikationsdatum der Erstveröffentlichung: 12 Februar 2024
Verlag: ACS
Titel der Zeitschrift, Zeitung oder Schriftenreihe: Langmuir
Jahrgang/Volume einer Zeitschrift: 40
(Heft-)Nummer: 8
Kollation: 28 Seiten
DOI: 10.26083/tuprints-00026753
URL / URN: https://tuprints.ulb.tu-darmstadt.de/26753
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Herkunft: Zweitveröffentlichungsservice
Kurzbeschreibung (Abstract):

An approach for direct in-pore solid-phase ultrashort peptide synthesis on mesoporous films using the amino acids arginine, leucine, and glycine is presented. Although the number of grafted amino acids remains low, the ionic mesopore accessibility can be gradually adjusted. The addition of arginine in up to five reaction cycles leads to a progressive increase in positive mesopore charge density, which gradually increases the anionic mesopore accessibility at acidic pH. At basic pH, the remaining silanol groups at the pore wall still dominate counter-charged cation mesopore accessibility. Thus, specific peptide sequence design is demonstrated to be a sensitive tool for molecular transport control in nanoscale pores. Overall, the direct in-pore solid-phase ultrashort peptide synthesis on mesoporous films using the sequences of different amino acids opens up exciting opportunities for the development of innovative materials with precisely tailored properties and functions based on specific peptide sequence design.

Freie Schlagworte: short peptide, ion transport, solid-phase peptide synthesis, biofunctionalization, BODIPY, mesoporous silica, nanopores
Status: Postprint
URN: urn:nbn:de:tuda-tuprints-267538
Sachgruppe der Dewey Dezimalklassifikatin (DDC): 500 Naturwissenschaften und Mathematik > 540 Chemie
Fachbereich(e)/-gebiet(e): 07 Fachbereich Chemie
07 Fachbereich Chemie > Ernst-Berl-Institut
07 Fachbereich Chemie > Ernst-Berl-Institut > Fachgebiet Makromolekulare Chemie
Hinterlegungsdatum: 30 Apr 2024 12:35
Letzte Änderung: 02 Mai 2024 07:33
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