A self-assembling peptide RADA16-I integrated with spider fibroin uncrystalline motifs

Lijuan Sun1,2, Xiaojun Zhao1,31West China Hospital Laboratory of Nanomedicine and Institute for Nanobiomedical Technology and Membrane Biology, Sichuan University, Chengdu 610041, Sichuan, China; 2Dept of Oral and Maxillofacial Surgery, Sun Yat-sen Memorial Hospital, Sun Yat-sen University, Guangzho...

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Autores principales:	Sun L, Zhao X
Formato:	article
Lenguaje:	EN
Publicado:	Dove Medical Press 2012
Materias:	Medicine (General) R5-920
Acceso en línea:	https://doaj.org/article/99d8b20ac89541e6bf6babf815e3bcae
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spelling	oai:doaj.org-article:99d8b20ac89541e6bf6babf815e3bcae2021-12-02T00:53:27ZA self-assembling peptide RADA16-I integrated with spider fibroin uncrystalline motifs1176-91141178-2013https://doaj.org/article/99d8b20ac89541e6bf6babf815e3bcae2012-02-01T00:00:00Zhttp://www.dovepress.com/a-self-assembling-peptide-rada16-i-integrated-with-spider-fibroin-uncr-a9196https://doaj.org/toc/1176-9114https://doaj.org/toc/1178-2013Lijuan Sun1,2, Xiaojun Zhao1,31West China Hospital Laboratory of Nanomedicine and Institute for Nanobiomedical Technology and Membrane Biology, Sichuan University, Chengdu 610041, Sichuan, China; 2Dept of Oral and Maxillofacial Surgery, Sun Yat-sen Memorial Hospital, Sun Yat-sen University, Guangzhou 510120, Guangdong, China; 3Center for Biomedical Engineering NE47-378, Massachusetts Institute of Technology, Cambridge, MA 02139-4307, USAAbstract: Mechanical strength of nanofiber scaffolds formed by the self-assembling peptide RADA16-I or its derivatives is not very good and limits their application. To address this problem, we inserted spidroin uncrystalline motifs, which confer incomparable elasticity and hydrophobicity to spider silk GGAGGS or GPGGY, into the C-terminus of RADA16-I to newly design two peptides: R3 (n-RADARADARADARADA-GGAGGS-c) and R4 (n-RADARADARADARADA-GPGGY-c), and then observed the effect of these motifs on biophysical properties of the peptide. Atomic force microscopy, transmitting electron microscopy, and circular dichroism spectroscopy confirm that R3 and R4 display &szlig;-sheet structure and self-assemble into long nanofibers. Compared with R3, the &szlig;-sheet structure and nanofibers formed by R4 are more stable; they change to random coil and unordered aggregation at higher temperature. Rheology measurements indicate that novel peptides form hydrogel when induced by DMEM, and the storage modulus of R3 and R4 hydrogel is 0.5 times and 3 times higher than that of RADA16-I, respectively. Furthermore, R4 hydrogel remarkably promotes growth of liver cell L02 and liver cancer cell SMCC7721 compared with 2D culture, determined by MTT assay. Novel peptides still have potential as hydrophobic drug carriers; they can stabilize pyrene microcrystals in aqueous solution and deliver this into a lipophilic environment, identified by fluorescence emission spectra. Altogether, the spider fibroin motif GPGGY most effectively enhances mechanical strength and hydrophobicity of the peptide. This study provides a new method in the design of nanobiomaterials and helps us to understand the role of the amino acid sequence in nanofiber formation.Keywords: uncrystalline motif, self-assembling peptide, &szlig;-sheet, nanofiber, mechanical strength, hydrophobic compound carrierSun LZhao XDove Medical PressarticleMedicine (General)R5-920ENInternational Journal of Nanomedicine, Vol 2012, Iss default, Pp 571-580 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine (General) R5-920
spellingShingle	Medicine (General) R5-920 Sun L Zhao X A self-assembling peptide RADA16-I integrated with spider fibroin uncrystalline motifs
description	Lijuan Sun1,2, Xiaojun Zhao1,31West China Hospital Laboratory of Nanomedicine and Institute for Nanobiomedical Technology and Membrane Biology, Sichuan University, Chengdu 610041, Sichuan, China; 2Dept of Oral and Maxillofacial Surgery, Sun Yat-sen Memorial Hospital, Sun Yat-sen University, Guangzhou 510120, Guangdong, China; 3Center for Biomedical Engineering NE47-378, Massachusetts Institute of Technology, Cambridge, MA 02139-4307, USAAbstract: Mechanical strength of nanofiber scaffolds formed by the self-assembling peptide RADA16-I or its derivatives is not very good and limits their application. To address this problem, we inserted spidroin uncrystalline motifs, which confer incomparable elasticity and hydrophobicity to spider silk GGAGGS or GPGGY, into the C-terminus of RADA16-I to newly design two peptides: R3 (n-RADARADARADARADA-GGAGGS-c) and R4 (n-RADARADARADARADA-GPGGY-c), and then observed the effect of these motifs on biophysical properties of the peptide. Atomic force microscopy, transmitting electron microscopy, and circular dichroism spectroscopy confirm that R3 and R4 display &szlig;-sheet structure and self-assemble into long nanofibers. Compared with R3, the &szlig;-sheet structure and nanofibers formed by R4 are more stable; they change to random coil and unordered aggregation at higher temperature. Rheology measurements indicate that novel peptides form hydrogel when induced by DMEM, and the storage modulus of R3 and R4 hydrogel is 0.5 times and 3 times higher than that of RADA16-I, respectively. Furthermore, R4 hydrogel remarkably promotes growth of liver cell L02 and liver cancer cell SMCC7721 compared with 2D culture, determined by MTT assay. Novel peptides still have potential as hydrophobic drug carriers; they can stabilize pyrene microcrystals in aqueous solution and deliver this into a lipophilic environment, identified by fluorescence emission spectra. Altogether, the spider fibroin motif GPGGY most effectively enhances mechanical strength and hydrophobicity of the peptide. This study provides a new method in the design of nanobiomaterials and helps us to understand the role of the amino acid sequence in nanofiber formation.Keywords: uncrystalline motif, self-assembling peptide, &szlig;-sheet, nanofiber, mechanical strength, hydrophobic compound carrier
format	article
author	Sun L Zhao X
author_facet	Sun L Zhao X
author_sort	Sun L
title	A self-assembling peptide RADA16-I integrated with spider fibroin uncrystalline motifs
title_short	A self-assembling peptide RADA16-I integrated with spider fibroin uncrystalline motifs
title_full	A self-assembling peptide RADA16-I integrated with spider fibroin uncrystalline motifs
title_fullStr	A self-assembling peptide RADA16-I integrated with spider fibroin uncrystalline motifs
title_full_unstemmed	A self-assembling peptide RADA16-I integrated with spider fibroin uncrystalline motifs
title_sort	self-assembling peptide rada16-i integrated with spider fibroin uncrystalline motifs
publisher	Dove Medical Press
publishDate	2012
url	https://doaj.org/article/99d8b20ac89541e6bf6babf815e3bcae
work_keys_str_mv	AT sunl aselfassemblingpeptiderada16iintegratedwithspiderfibroinuncrystallinemotifs AT zhaox aselfassemblingpeptiderada16iintegratedwithspiderfibroinuncrystallinemotifs AT sunl selfassemblingpeptiderada16iintegratedwithspiderfibroinuncrystallinemotifs AT zhaox selfassemblingpeptiderada16iintegratedwithspiderfibroinuncrystallinemotifs
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A self-assembling peptide RADA16-I integrated with spider fibroin uncrystalline motifs

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