Exploring the potency of the naturally occurring polyphenol curcumin as a probe for protein aggregation in crowded environments

被引:4
|
作者
Karmakar, Sandip [1 ]
Chakraborty, Saikat [1 ]
Gautam, Saurabh [1 ]
Chowdhury, Pramit K. [1 ]
机构
[1] Indian Inst Technol Delhi, Dept Chem, New Delhi 110016, India
关键词
THIOFLAVIN-T BINDING; HUMAN SERUM-ALBUMIN; UNFOLDED STATES; FIBRILS; SOLUBILITY; STABILITY; CYCLODEXTRINS; PROTOFIBRILS; FIBRILLATION; DYNAMICS;
D O I
10.1016/j.ijbiomac.2019.09.049
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Conventional dyes such as thioflavin T, ANS, and Congo Red etc. have mostly been used to monitor protein aggregation. In this work, we have tried the naturally occurring polyphenol, curcumin, for probing the aggregation of the serum protein bovine serum albumin (BSA) in crowded environments. The distinctive spectral profile of this polyphenol in response to varying aggregating scenario is indicative of its high sensitivity towards detection of aggregates. We have also gained possible insights into the heterogeneity of the aggregation mixture, that is, the different species that are present simultaneously at any instant of time by fitting curcumin's emission spectra to a sum of Gaussians in diverse aggregating conditions. SEM study reveals that the morphology of aggregates formed in presence of different crowding agents became independent of the nature of the crowder on prolonged incubation. To overcome the aqueous insolubility barrier of the molecular probe (curcumin), beta-cyclodextrin, which is known to complex with curcumin, was also added to the reaction mixture. (C) 2019 Elsevier B.V. All rights reserved.
引用
收藏
页码:1088 / 1101
页数:14
相关论文
共 13 条
  • [1] Protein aggregation in crowded environments
    Ellis, R. John
    Minton, Allen P.
    BIOLOGICAL CHEMISTRY, 2006, 387 (05) : 485 - 497
  • [2] Protein Aggregation in Crowded Environments
    White, Duncan A.
    Buell, Alexander K.
    Knowles, Tuomas P. J.
    Welland, Mark E.
    Dobson, Christopher M.
    JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2010, 132 (14) : 5170 - 5175
  • [3] Protein Folding and Aggregation - From Crowded Environments into the Cell
    Ebbinghaus, Simon
    BIOPHYSICAL JOURNAL, 2014, 106 (02) : 736A - 736A
  • [4] The Role of Crowded Physiological Environments in Prion and Prion-like Protein Aggregation
    Ma, Qian
    Hu, Ji-Ying
    Chen, Jie
    Liang, Yi
    INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 2013, 14 (11): : 21339 - 21352
  • [5] Specific Ion Effects on Protein Thermal Aggregation from Dilute Solutions to Crowded Environments
    Li, Shuling
    Ye, Shuji
    Liu, Guangming
    LANGMUIR, 2018, 34 (14) : 4289 - 4297
  • [6] Modulation of prion protein folding and aggregation state by naturally occurring small molecule compounds
    Stroylova, Y.
    Tishina, S.
    Stroylov, V.
    Melnikova, A.
    Muronetz, V.
    FEBS JOURNAL, 2017, 284 : 214 - 214
  • [7] Exploring Weak, Transient Protein-Protein Interactions in Crowded In Vivo Environments by In-Cell Nuclear Magnetic Resonance Spectroscopy
    Wang, Qinghua
    Zhuravleva, Anastasia
    Gierasch, Lila M.
    BIOCHEMISTRY, 2011, 50 (43) : 9225 - 9236
  • [8] Aggregation-prone peptides modulate activity of bovine interferon gamma released from naturally occurring protein nanoparticles
    Vicente Carratala, Jose
    Cano-Garrido, Olivia
    Sanchez, Julieta
    Membrado, Cristina
    Perez, Eudald
    Conchillo-Sole, Oscar
    Daura, Xavier
    Sanchez-Chardi, Alejandro
    Villaverde, Antonio
    Aris, Anna
    Garcia-Fruitos, Elena
    Ferrer-Miralles, Neus
    NEW BIOTECHNOLOGY, 2020, 57 (57) : 11 - 19
  • [9] In vitro expression of 34 naturally occurring mutant variants of phenylalanine hydroxylase:: Correlation with metabolic phenotypes and susceptibility toward protein aggregation
    Gjetting, T
    Petersen, M
    Guldberg, P
    Güttler, F
    MOLECULAR GENETICS AND METABOLISM, 2001, 72 (02) : 132 - 143
  • [10] Naturally occurring NOTCH3 exon skipping attenuates NOTCH3 protein aggregation and disease severity in CADASIL patients
    Gravesteijn, Gido
    Dauwerse, Johannes G.
    Overzier, Maurice
    Brouwer, Gwendolyn
    Hegeman, Ingrid
    Mulder, Aat A.
    Baas, Frank
    Kruit, Mark C.
    Terwindt, Gisela M.
    van Duinen, Sjoerd G.
    Jost, Carolina R.
    Aartsma-Rus, Annemieke
    Oberstein, Saskia A. J. Lesnik
    Rutten, Julie W.
    HUMAN MOLECULAR GENETICS, 2020, 29 (11) : 1853 - 1863