NDLI: Alkyl chain grafted poly(l-lysine): self-assembly and biomedical application as carriers

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Alkyl chain grafted poly(l-lysine): self-assembly and biomedical application as carriers

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Back cover

Soft Matter Vol - 7 Issue - 7

Soft Matter Vol - 7 Issue - 6

Soft Matter Vol - 7 Issue - 5

Soft Matter Vol - 7 Issue - 4

Soft Matter Vol - 7 Issue - 3

Alkyl chain grafted poly(l-lysine): self-assembly and biomedical application as carriers

Content Provider	Royal Society of Chemistry (RSC)
Author	Huang, Yun-Chiao Jan, Jeng-Shiung Arham, Marannu
Copyright Year	2011
Abstract	The synthesis and self-assembly of amphiphilic copolypeptides, poly(L-lysine)-graft-hexanoyl (PLH), and their evaluation as carriers/encapsulants for myoglobin (Mb) encapsulation have been investigated. The interplay between the hydrophobic interaction and the chain conformational changes upon hexanoyl substitution determined the self-assembly behavior of PLH, which further influenced the evolution of the assembled nanostructures. The experimental data revealed that vesicles with mean sizes between 100 and 500 nm were formed by these amphiphilic copolypeptides in acidic and neutral aqueous solution. The hexanoyl substitution can regulate the hydrophobic interaction, chain conformation of PLH, and subsequently the size of the assembled vesicles at different pH. Taking advantage of the self-assembly capability, the PLH was employed for protein encapsulation, i.e.myoglobin (Mb). The encapsulation efficiency was higher than 50% and the encapsulated protein was still capable of carrying oxygen, which demonstrated that the PLH vesicles are promising carriers or encapsulants. The Mb-loaded PLH particles were further crosslinked by genipin to form stable nanostructures with mean sizes between 180 and 280 nm. The as-prepared particles were found to be well suspended in solution for months. With versatility of this synthesis strategy, additional functionality can be incorporated on PLH, which can allow these amphiphilic copolypeptides to be useful as targeted drug carriers, biomimetic encapsulants, and functional nanobioreactors in the biomedical fields.
Starting Page	3975
Ending Page	3983
Page Count	9
File Format	HTM / HTML PDF
ISSN	1744683X
Volume Number	7
Issue Number	8
Journal	Soft Matter
DOI	10.1039/c0sm01034k
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Myoglobin Self-assembly Oxygen Biomimetics Lysine Interplay Entertainment Amphiphile Hydrophobe Protein structure Protein Genipin
Content Type	Text
Resource Type	Article
Subject	Chemistry Condensed Matter Physics

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