Coacervation of resilin fusion proteins containing terminal functionalities

Wenwen Fang; null 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^*

^*Tämän työn vastaava kirjoittaja

VTT Technical Research Centre of Finland Ltd.

Tutkimustuotos: Lehtiartikkeli › Article › Scientific › vertaisarvioitu

10 Sitaatiot (Scopus)

165 Lataukset (Pure)

Abstrakti

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.

Alkuperäiskieli	Englanti
Sivut	590-596
Sivumäärä	7
Julkaisu	Colloids and Surfaces B: Biointerfaces
Vuosikerta	171
DOI - pysyväislinkit	https://doi.org/10.1016/j.colsurfb.2018.07.048
Tila	Julkaistu - 1 marrask. 2018
OKM-julkaisutyyppi	A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä

Pääsy asiakirjaan

10.1016/j.colsurfb.2018.07.048

Coacervation ElsevierAccepted author manuscript, 784 KBLisenssi: CC BY-NC-ND

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Link to publication in Scopus

HYBER: Suomen Akatemian Biosynteettisten hybridimateriaalien molekyylimuokkauksen huippuyksikkö (2014-2019)
Ikkala, O. (Vastuullinen tutkija)
01/01/2017 → 31/12/2019
Projekti: Academy of Finland: Other research funding

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@article{99746175e0e14ba6897529f4c700d5c7,

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 = "Resilin, Self-assembly, Coacervation, Selective adhesion, Tomography, TROPOELASTIN, HYDROPHOBINS, CELLULOSE, REC1-RESILIN, GRAPHENE",

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",

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",

issn = "0927-7765",

publisher = "Elsevier",

}

TY - JOUR

T1 - Coacervation of resilin fusion proteins containing terminal functionalities

AU - Fang, Wenwen

AU - Nonappa, null

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 - Resilin

KW - Self-assembly

KW - Coacervation

KW - Selective adhesion

KW - Tomography

KW - TROPOELASTIN

KW - HYDROPHOBINS

KW - CELLULOSE

KW - REC1-RESILIN

KW - GRAPHENE

UR - http://www.scopus.com/inward/record.url?scp=85051129916&partnerID=8YFLogxK

U2 - 10.1016/j.colsurfb.2018.07.048

DO - 10.1016/j.colsurfb.2018.07.048

M3 - Article

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

Abstrakti

Pääsy asiakirjaan

Muut tiedostot ja linkit

Sormenjälki

Projektit

HYBER: Suomen Akatemian Biosynteettisten hybridimateriaalien molekyylimuokkauksen huippuyksikkö (2014-2019)

Laitteet

Biotalousinfrastruktuuri

OtaNano

OtaNano Nanomikroskopiakeskus

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