Designing unconventional Fmoc-peptide-based biomaterials: structure and related properties

We have recently employed l -amino acids in the lipase-catalyzed biofabrication of a class of self-assembling Fmoc-peptides that form 3-dimensional nanofiber scaffolds. Here we report that using d -amino acids, the homochiral self-assembling peptide Fmoc- d -Phe 3 (Fmoc-F*F*F*) also forms a 3-dimens...

Full description

Saved in:
Bibliographic Details
Published in:Soft matter 2014-03, Vol.1 (12), p.1944-1952
Main Authors: Chronopoulou, Laura, Sennato, Simona, Bordi, Federico, Giannella, Domenico, Di Nitto, Antonio, Barbetta, Andrea, Dentini, Mariella, Togna, Anna Rita, Togna, Giuseppina Ines, Moschini, Sabina, Palocci, Cleofe
Format: Article
Language:English
Subjects:
Amino Acids - chemistry
Biocompatible Materials - chemistry
Biocompatible Materials - pharmacology
Biomedical materials
Cell Survival - drug effects
Controlled release
Dichroism
Hydrogel, Polyethylene Glycol Dimethacrylate - chemistry
Hydrogel, Polyethylene Glycol Dimethacrylate - pharmacology
Kinetics
Microscopy, Atomic Force
Models, Molecular
Nanofibers - chemistry
Nanoparticles
Nanostructure
Peptides
Peptides - chemistry
Peptides - pharmacology
Scaffolds
Surgical implants
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:We have recently employed l -amino acids in the lipase-catalyzed biofabrication of a class of self-assembling Fmoc-peptides that form 3-dimensional nanofiber scaffolds. Here we report that using d -amino acids, the homochiral self-assembling peptide Fmoc- d -Phe 3 (Fmoc-F*F*F*) also forms a 3-dimensional nanofiber scaffold that is substantially distinguishable from its l -peptide and heterochiral peptide (F*FF and FF*F*) counterparts on the basis of their physico-chemical properties. Such chiral peptides self-assemble into ordered nanofibers with well defined fibrillar motifs. Circular dichroism and atomic force microscopy have been employed to study in depth such fibrillar peptide structures. Dexamethasone release kinetics from PLGA and CS-PLGA nanoparticles entrapped within the peptidic hydrogel matrix encourage its use for applications in drug controlled release. In this work we investigate the effect of chirality on the biosynthesis of self-assembling peptides and on the structure-performance relationships of the resulting hydrogels.
ISSN:1744-683X
1744-6848
DOI:10.1039/c3sm52457d