Small amphipathic peptides are responsible for the assembly of cruciferin nanoparticles

Abstract Amphipathic peptides are versatile building blocks for fabricating well-ordered nanostructures, which have gained much attention owing to their enormous design possibilities and bio-functionalities. However, using amphipathic peptides from natural proteins to create tunable nanostructures i...

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Autores principales:	Hui Hong, Ali Akbari, Jianping Wu
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/edd0d0cd9ea8497da9a8b2d73c9c0fcf
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spelling	oai:doaj.org-article:edd0d0cd9ea8497da9a8b2d73c9c0fcf2021-12-02T16:06:25ZSmall amphipathic peptides are responsible for the assembly of cruciferin nanoparticles10.1038/s41598-017-07908-z2045-2322https://doaj.org/article/edd0d0cd9ea8497da9a8b2d73c9c0fcf2017-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-07908-zhttps://doaj.org/toc/2045-2322Abstract Amphipathic peptides are versatile building blocks for fabricating well-ordered nanostructures, which have gained much attention owing to their enormous design possibilities and bio-functionalities. However, using amphipathic peptides from natural proteins to create tunable nanostructures is challenging because of their heterogeneity and great tendency to form aggregates. Here we fabricated two well-defined nanoparticles from cruciferin amphipathic peptides by integrating top-down and bottom-up approach. Alkali hydrolysis (pH 12, 120 °C for 30 min) was introduced to break down intact cruciferin into peptides (top–down). The cruciferin peptides and their fractions were then assembled into nanoparticles (bottom–up) in the presence of calcium ions. The permeate fraction from 10 kDa cut-off membrane formed smaller nanoparticles (F1-NPs) (around 82 nm) than that of unfractionated cruciferin peptides (CRU-NPs, around 185 nm); the electrostatic and hydrophobic interactions were the main driving forces for particle formation. LC-MS/MS analysis characterised that the small amphipathic peptides (Xn1Zn2Xn3Zn4, n1–4 = 0~5), composed of alternating hydrophobic (X) and hydrophilic (Z) amino acid with a length of 5–15 and 5–20 residues for F1-NPs and CRU-NPs, respectively, were responsible for particle formation. Our study established the mechanism of particle formation of the cold gelation is through assembly of amphipathic peptides.Hui HongAli AkbariJianping WuNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-13 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Hui Hong Ali Akbari Jianping Wu Small amphipathic peptides are responsible for the assembly of cruciferin nanoparticles
description	Abstract Amphipathic peptides are versatile building blocks for fabricating well-ordered nanostructures, which have gained much attention owing to their enormous design possibilities and bio-functionalities. However, using amphipathic peptides from natural proteins to create tunable nanostructures is challenging because of their heterogeneity and great tendency to form aggregates. Here we fabricated two well-defined nanoparticles from cruciferin amphipathic peptides by integrating top-down and bottom-up approach. Alkali hydrolysis (pH 12, 120 °C for 30 min) was introduced to break down intact cruciferin into peptides (top–down). The cruciferin peptides and their fractions were then assembled into nanoparticles (bottom–up) in the presence of calcium ions. The permeate fraction from 10 kDa cut-off membrane formed smaller nanoparticles (F1-NPs) (around 82 nm) than that of unfractionated cruciferin peptides (CRU-NPs, around 185 nm); the electrostatic and hydrophobic interactions were the main driving forces for particle formation. LC-MS/MS analysis characterised that the small amphipathic peptides (Xn1Zn2Xn3Zn4, n1–4 = 0~5), composed of alternating hydrophobic (X) and hydrophilic (Z) amino acid with a length of 5–15 and 5–20 residues for F1-NPs and CRU-NPs, respectively, were responsible for particle formation. Our study established the mechanism of particle formation of the cold gelation is through assembly of amphipathic peptides.
format	article
author	Hui Hong Ali Akbari Jianping Wu
author_facet	Hui Hong Ali Akbari Jianping Wu
author_sort	Hui Hong
title	Small amphipathic peptides are responsible for the assembly of cruciferin nanoparticles
title_short	Small amphipathic peptides are responsible for the assembly of cruciferin nanoparticles
title_full	Small amphipathic peptides are responsible for the assembly of cruciferin nanoparticles
title_fullStr	Small amphipathic peptides are responsible for the assembly of cruciferin nanoparticles
title_full_unstemmed	Small amphipathic peptides are responsible for the assembly of cruciferin nanoparticles
title_sort	small amphipathic peptides are responsible for the assembly of cruciferin nanoparticles
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/edd0d0cd9ea8497da9a8b2d73c9c0fcf
work_keys_str_mv	AT huihong smallamphipathicpeptidesareresponsiblefortheassemblyofcruciferinnanoparticles AT aliakbari smallamphipathicpeptidesareresponsiblefortheassemblyofcruciferinnanoparticles AT jianpingwu smallamphipathicpeptidesareresponsiblefortheassemblyofcruciferinnanoparticles
_version_	1718384999354335232

Small amphipathic peptides are responsible for the assembly of cruciferin nanoparticles

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