𝔖 Bobbio Scriptorium
✦   LIBER   ✦

In situ cross-linking of the shell of self-assembled peptide nanotubes

✍ Scribed by Rhishikesh Gokhale; Julien Couet; Markus Biesalski


Publisher
John Wiley and Sons
Year
2010
Tongue
English
Weight
564 KB
Volume
207
Category
Article
ISSN
0031-8965

No coin nor oath required. For personal study only.

✦ Synopsis


Abstract

Peptide polymer nanotubes (PPNTs) were prepared by in situ surface‐initiated atom transfer radical polymerization (ATRP) from self‐assembled cyclic peptide nanotubes. PPNT dimensions, i.e., height (i.e. diameter) and length, as derived from AFM measurements of surface‐adsorbed, dry PPNT are a function of the molar mass of the peptide‐attached polymer molecules, and the overall structure is determined by subtle interplay of peptide–peptide and polymer–polymer interactions. As shown in previous communications, a PPNT length reduction occurs with increasing grafted mass of polymer chains. The latter may be attributed to strong segment–segment interactions of the nanotube‐grafted macromolecules. Here, we introduce a possible strategy to chemically stabilize PPNT. Peptide‐polymer nanotubes are prepared by in situ cross‐linking of the polymeric shell using the bi‐functional monomer ethylene glycol dimethacrylate (EGDMA) during surface‐initiated polymerization. PEGDMA‐PPNTs were characterized with respect to chemical identity, chemical stability and structure in the dry state, using FTIR, dissolution assays, and atomic force microscope (AFM) cross‐section analysis, respectively. The use of the cross‐linkable monomer yields chemically stable rigid‐rod like hybrid materials, where the overall length of the nano‐objects remains at a constant value of about 100 nm regardless of the adsorbed mass of the nanotube‐surrounding polymer material.


📜 SIMILAR VOLUMES


In situ polymerization of tropoelastin i
✍ Suzanne M. Mithieux; Yidong Tu; Emine Korkmaz; Filip Braet; Anthony S. Weiss 📂 Article 📅 2009 🏛 Elsevier Science 🌐 English ⚖ 537 KB

Tropoelastin, the polypeptide monomer precursor of elastin, is covalently cross-linked to give stable elastic structures. We show here that elastic biomaterials can be generated from tropoelastin in the absence of the classically accepted cross-linking pathway. Under alkaline conditions tropoelastin