Coacervation of resilin fusion proteins containing terminal functionalities

Wenwen Fang; Nonappa; Marika Vitikainen; Pezhman Mohammadi; Salla Koskela; Miika Soikkeli; Ann Westerholm-Parvinen; Christopher P. Landowski; Merja Penttilä; Markus B. Linder; Päivi Laaksonen

doi:10.1016/j.colsurfb.2018.07.048

Coacervation of resilin fusion proteins containing terminal functionalities

Wenwen Fang
, Nonappa
, Marika Vitikainen
, Pezhman Mohammadi
, Salla Koskela
, Miika Soikkeli
, Ann Westerholm-Parvinen
, Christopher P. Landowski
, Merja Penttilä
, Markus B. Linder
, Päivi Laaksonen^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › Scientific › peer-review

11 Citations (Scopus)

Abstract

Liquid-liquid phase transition known as coacervation of resilin-like-peptide fusion proteins containing different terminal domains were investigated. Two different modular proteins were designed and produced and their behavior were compared to a resilin-like-peptide without terminal domains. The size of the particle-like coacervates was modulated by the protein concentration, pH and temperature. The morphology and three-dimensional (3D) structural details of the coacervate particles were investigated by cryogenic transmission electron microscopy (cryo-TEM) and tomography (cryo-ET) reconstruction. Selective adhesion of the coacervates on cellulose and graphene surfaces was demonstrated.

Original language	English
Pages (from-to)	590-596
Journal	Colloids and Surfaces B: Biointerfaces
Volume	171
DOIs	https://doi.org/10.1016/j.colsurfb.2018.07.048
Publication status	Published - 1 Nov 2018
MoE publication type	A1 Journal article-refereed

Funding

The authors acknowledge the Academy of Finland Center of Excellence Program, especially the Center of Excellence in Molecular Engineering of Biosynthetic Hybrid Materials (HYBER). This work made use of the facilities at the Aalto University Nanomicroscopy Center (Aalto-NMC) premises.

Keywords

Coacervation
Resilin
Selective adhesion
Self-assembly
Tomography

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10.1016/j.colsurfb.2018.07.048

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title = "Coacervation of resilin fusion proteins containing terminal functionalities",

abstract = "Liquid-liquid phase transition known as coacervation of resilin-like-peptide fusion proteins containing different terminal domains were investigated. Two different modular proteins were designed and produced and their behavior were compared to a resilin-like-peptide without terminal domains. The size of the particle-like coacervates was modulated by the protein concentration, pH and temperature. The morphology and three-dimensional (3D) structural details of the coacervate particles were investigated by cryogenic transmission electron microscopy (cryo-TEM) and tomography (cryo-ET) reconstruction. Selective adhesion of the coacervates on cellulose and graphene surfaces was demonstrated.",

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T1 - Coacervation of resilin fusion proteins containing terminal functionalities

AU - Fang, Wenwen

AU - Nonappa,

AU - Vitikainen, Marika

AU - Mohammadi, Pezhman

AU - Koskela, Salla

AU - Soikkeli, Miika

AU - Westerholm-Parvinen, Ann

AU - Landowski, Christopher P.

AU - Penttilä, Merja

AU - Linder, Markus B.

AU - Laaksonen, Päivi

PY - 2018/11/1

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N2 - Liquid-liquid phase transition known as coacervation of resilin-like-peptide fusion proteins containing different terminal domains were investigated. Two different modular proteins were designed and produced and their behavior were compared to a resilin-like-peptide without terminal domains. The size of the particle-like coacervates was modulated by the protein concentration, pH and temperature. The morphology and three-dimensional (3D) structural details of the coacervate particles were investigated by cryogenic transmission electron microscopy (cryo-TEM) and tomography (cryo-ET) reconstruction. Selective adhesion of the coacervates on cellulose and graphene surfaces was demonstrated.

AB - Liquid-liquid phase transition known as coacervation of resilin-like-peptide fusion proteins containing different terminal domains were investigated. Two different modular proteins were designed and produced and their behavior were compared to a resilin-like-peptide without terminal domains. The size of the particle-like coacervates was modulated by the protein concentration, pH and temperature. The morphology and three-dimensional (3D) structural details of the coacervate particles were investigated by cryogenic transmission electron microscopy (cryo-TEM) and tomography (cryo-ET) reconstruction. Selective adhesion of the coacervates on cellulose and graphene surfaces was demonstrated.

KW - Coacervation

KW - Resilin

KW - Selective adhesion

KW - Self-assembly

KW - Tomography

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M3 - Article

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AN - SCOPUS:85051129916

SN - 0927-7765

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SP - 590

EP - 596

JO - Colloids and Surfaces B: Biointerfaces

JF - Colloids and Surfaces B: Biointerfaces

ER -

Coacervation of resilin fusion proteins containing terminal functionalities

Abstract

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Keywords

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