The effect of NaCl on the self-assembly of elastin-like block co-recombinamers: Tuning the size of micelles and vesicles

被引:19
|
作者
Pinedo-Martin, Guillermo [1 ]
Santos, Mercedes [1 ]
Testera, Ana M. [1 ]
Alonso, Matilde [1 ]
Carlos Rodriguez-Cabello, J. [1 ]
机构
[1] Univ Valladolid, Bioforge Grp, E-47011 Valladolid, Spain
关键词
Elastin-like; Salt; Nanoparticles; INVERSE TEMPERATURE TRANSITION; DRUG-DELIVERY; TRIBLOCK COPOLYMERS; SECONDARY STRUCTURE; AQUEOUS-SOLUTIONS; NANOPARTICLES; POLYMERS; MICELLIZATION; POLYPEPTIDES; SALTS;
D O I
10.1016/j.polymer.2014.08.053
中图分类号
O63 [高分子化学(高聚物)];
学科分类号
070305 ; 080501 ; 081704 ;
摘要
Herein we present a study of the effect of the addition of NaCl on the size and shape of thermally driven elastin-like block co-recombinamer (ELbcRs) self-assembled nano-objects. Many researchers are currently using NaCl to tune the transition temperature (T-t) of elastin-like recombinamers (ELRs). However, this method is used without a complete understanding of the potential changes in the self-assembly process that might result. Therefore, although salts other than NaCl are used for comparison in this study, the main effort is directed towards the effect of NaCl as this salt is widely and routinely used to control T-t in ELR purification protocols and their applications. Dynamic light scattering (DLS) was used to follow the formation and determine the size of the nano-objects assembled, whereas static light scattering (SLS) was performed to study the molecular weight and gyration radius of the aggregates. Cryo-transmission electron microscopy (Cryo-TEM) was used to corroborate the data obtained by light scattering. These results support the use of NaCl as a highly interesting means of controlling the dimensions of ELbcR-based self-assembled nanoparticles in aqueous solution. (C) 2014 Elsevier Ltd. All rights reserved.
引用
收藏
页码:5314 / 5321
页数:8
相关论文
共 50 条
  • [21] Self-Assembly Behavior of Elastin-like Polypeptide Diblock Copolymers Containing a Charged Moiety
    Choi, Jeong-Wan
    Choi, Soo-Hyung
    Won, Jong-In
    BIOMACROMOLECULES, 2021, 22 (06) : 2604 - 2613
  • [22] Structure and Self-Assembly of Elastin-Like Peptides: A Joint Molecular Dynamics and NMR Study
    Huynh, Q.
    Reichheld, S.
    Rauscher, S.
    Sharpe, S.
    Pomes, R.
    EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS, 2017, 46 : S395 - S395
  • [23] Thermoresponsive self-assembly of short elastin-like polypentapeptides and their poly(ethylene glycol) derivatives
    Pechar, Michal
    Brus, Jiri
    Kostka, Libor
    Konak, Cestmir
    Urbanova, Martina
    Slouf, Miroslav
    MACROMOLECULAR BIOSCIENCE, 2007, 7 (01) : 56 - 69
  • [24] Structure and Self-Assembly of Elastin-Like Peptides: A Joint Molecular Dynamics and NMR Study
    Pomes, Regis
    Huynh, Quang
    Reichheld, Sean
    Rauscher, Sarah
    Wu, Zhen Hao
    Sharpe, Simon
    PROTEIN SCIENCE, 2017, 26 : 119 - 120
  • [25] Self-Assembly of Monodisperse Oligonucleotide-Elastin Block Copolymers into Stars and Compound Micelles
    Fluegel, Sabine
    Buehler, Jasmin
    Fischer, Karl
    McDaniel, Jonathan R.
    Chilkoti, Ashutosh
    Schmidt, Manfred
    CHEMISTRY-A EUROPEAN JOURNAL, 2011, 17 (20) : 5503 - 5506
  • [26] Co-assembly behavior of oppositely charged thermoresponsive elastin-like polypeptide block copolymers
    Choi, Jeong-Wan
    Heo, Tae-Young
    Choi, Heelak
    Choi, Soo-Hyung
    Won, Jong-In
    JOURNAL OF APPLIED POLYMER SCIENCE, 2022, 139 (38)
  • [27] Double-hydrophobic elastin-like polypeptides with added functional motifs: Self-assembly and cytocompatibility
    Le, Duc H. T.
    Tsutsui, Yoko
    Sugawara-Narutaki, Ayae
    Yukawa, Hiroshi
    Baba, Yoshinobu
    Ohtsuki, Chikara
    JOURNAL OF BIOMEDICAL MATERIALS RESEARCH PART A, 2017, 105 (09) : 2475 - 2484
  • [28] Self-assembly/disassembly hysteresis of nanoparticles composed of marginally soluble, short elastin-like polypeptides
    Bahniuk, Markian S.
    Alshememry, Abdullah K.
    Elgersma, Scott V.
    Unsworth, Larry D.
    JOURNAL OF NANOBIOTECHNOLOGY, 2018, 16
  • [29] Structural determinants of cross-linking and hydrophobic domains for self-assembly of elastin-like polypeptides
    Miao, M
    Cirulis, JT
    Lee, S
    Keeley, FW
    BIOCHEMISTRY, 2005, 44 (43) : 14367 - 14375
  • [30] Sequence Control of the Self-Assembly of Elastin-Like Polypeptides into Hydrogels with Bespoke Viscoelastic and Structural Properties
    Barreiro, Diego Lopez
    Folch-Fortuny, Abel
    Muntz, Iain
    Thies, Jens C.
    Sagt, Cees M. J.
    Koenderink, Gijsje H.
    BIOMACROMOLECULES, 2022, 24 (01) : 489 - 501