Literature DB >> 17850149

Surface-assisted assembly of an ionic-complementary peptide: controllable growth of nanofibers.

Hong Yang1, Shan-Yu Fung, Mark Pritzker, P Chen.   

Abstract

Numerous studies have shown that a surface can direct and regulate molecular assembly. In this study, the nanofiber growth of an ionic-complementary peptide, EAK16-II, on a mica surface was investigated under various solution conditions via in situ atomic force microscopy. In comparison to the assembly in bulk solution, nanofiber growth of EAK16-II on mica is surface-assisted and involves two steps: (1) adsorption of nanofibers and fiber clusters (from the bulk solution) on the surface, serving as the "seeds"; (2) fiber elongation of the "seeds" from their active ends. The nanofiber growth can be controlled by adjusting the solution pH since it modulates the adsorption of the "seeds" on mica and their growth rates. The amount of the adsorbed "seeds" decreases with increasing solution pH, while the growth rate under different solution conditions is found to follow the order pure water > 1 mM HCl > 1 mM NaOH > 10 mM HCl approximately 10 mM NaOH approximately 0. The pH-dependent nanofiber growth is due to the surface charge of the peptides and peptide assemblies in various solutions as indicated by zeta-potential measurements. A simple model was proposed to describe surface-assisted nanofiber growth. This study provides insights into the assembly of peptide/protein on a surface, which is essential to understand such physiological protein aggregation systems as amyloid fibrillogenesis. In addition, the potential of this finding to construct biocompatible electrodes for biomolecular sensing is also discussed.

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Year:  2007        PMID: 17850149     DOI: 10.1021/ja073168u

Source DB:  PubMed          Journal:  J Am Chem Soc        ISSN: 0002-7863            Impact factor:   15.419


  10 in total

1.  Interaction of an ionic complementary peptide with a hydrophobic graphite surface.

Authors:  Yuebiao Sheng; Wei Wang; P Chen
Journal:  Protein Sci       Date:  2010-09       Impact factor: 6.725

2.  Mechanisms of the self-assembly of EAK16-family peptides into fibrillar and globular structures: molecular dynamics simulations from nano- to micro-seconds.

Authors:  Soheila Emamyari; Faezeh Kargar; Vahid Sheikh-Hasani; Saeed Emadi; Hossein Fazli
Journal:  Eur Biophys J       Date:  2015-04-02       Impact factor: 1.733

3.  All-atom molecular dynamics study of EAK16 peptide: the effect of pH on single-chain conformation, dimerization and self-assembly behavior.

Authors:  Soheila Emamyari; Hossein Fazli
Journal:  Eur Biophys J       Date:  2014-03-13       Impact factor: 1.733

4.  Nanomechanical stimulus accelerates and directs the self-assembly of silk-elastin-like nanofibers.

Authors:  Jonathan Chang; Xiu-Feng Peng; Karam Hijji; Joseph Cappello; Hamidreza Ghandehari; Santiago D Solares; Joonil Seog
Journal:  J Am Chem Soc       Date:  2011-01-19       Impact factor: 15.419

5.  Surface Induced nanofiber growth by self-assembly of a silk-elastin-like protein polymer.

Authors:  Wonseok Hwang; Bo-Hyun Kim; Ramesh Dandu; Joseph Cappello; Hamidreza Ghandehari; Joonil Seog
Journal:  Langmuir       Date:  2009-11-03       Impact factor: 3.882

6.  Effect of surfaces on amyloid fibril formation.

Authors:  Bradley Moores; Elizabeth Drolle; Simon J Attwood; Janet Simons; Zoya Leonenko
Journal:  PLoS One       Date:  2011-10-10       Impact factor: 3.240

7.  Nanoscopic and photonic ultrastructural characterization of two distinct insulin amyloid states.

Authors:  Katarzyna Maria Psonka-Antonczyk; Julien Duboisset; Bjørn Torger Stokke; Tamotsu Zako; Takahiro Kobayashi; Mizuo Maeda; Sofie Nyström; Jeff Mason; Per Hammarström; K Peter R Nilsson; Mikael Lindgren
Journal:  Int J Mol Sci       Date:  2012-02-01       Impact factor: 6.208

8.  Tailoring Peptide Self-Assembly and Formation of 2D Nanoribbons on Mica and HOPG Surface.

Authors:  Hao Kong; Bin Liu; Guozheng Yang; Yun Chen; Gang Wei
Journal:  Materials (Basel)       Date:  2022-01-02       Impact factor: 3.623

9.  Sequence effect of self-assembling peptides on the complexation and in vitro delivery of the hydrophobic anticancer drug ellipticine.

Authors:  Shan Yu Fung; Hong Yang; P Chen
Journal:  PLoS One       Date:  2008-04-09       Impact factor: 3.240

10.  Modification of hydrophilic and hydrophobic surfaces using an ionic-complementary peptide.

Authors:  Hong Yang; Shan-Yu Fung; Mark Pritzker; P Chen
Journal:  PLoS One       Date:  2007-12-19       Impact factor: 3.240

  10 in total

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