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

Helsinki University of Technology
VTT Technical Research Centre of Finland

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

11 Scopus citations

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
Number of pages	7
Journal	Colloids and Surfaces B: Biointerfaces
Volume	171
DOIs	https://doi.org/10.1016/j.colsurfb.2018.07.048
State	Published - 1 Nov 2018
Externally published	Yes

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.",

keywords = "Coacervation, Resilin, Selective adhesion, Self-assembly, Tomography",

author = "Wenwen Fang and Nonappa and Marika Vitikainen and Pezhman Mohammadi and Salla Koskela and Miika Soikkeli and Ann Westerholm-Parvinen and Landowski, \{Christopher P.\} and Merja Penttil{\"a} and Linder, \{Markus B.\} and P{\"a}ivi Laaksonen",

note = "Publisher Copyright: {\textcopyright} 2018 Elsevier B.V.",

year = "2018",

month = nov,

day = "1",

doi = "10.1016/j.colsurfb.2018.07.048",

language = "English",

volume = "171",

pages = "590--596",

journal = "Colloids and Surfaces B: Biointerfaces",

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publisher = "Elsevier B.V.",

}

TY - JOUR

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

Y1 - 2018/11/1

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

UR - https://www.scopus.com/pages/publications/85051129916

U2 - 10.1016/j.colsurfb.2018.07.048

DO - 10.1016/j.colsurfb.2018.07.048

M3 - Article

C2 - 30098537

AN - SCOPUS:85051129916

SN - 0927-7765

VL - 171

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

Keywords

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