Role of amino acid hydrophobicity, aromaticity, and molecular volume on IAPP(20-29) amyloid self-assembly

2012 ◽  
Vol 80 (4) ◽  
pp. 1053-1065 ◽  
Author(s):  
Todd M. Doran ◽  
Alissa J. Kamens ◽  
Nadia K. Byrnes ◽  
Bradley L. Nilsson
Keyword(s):  
Amino Acid ◽  
Self Assembly ◽  
Molecular Volume

Assembly of amino acid containing naphthalene diimide-based molecules: the role of intervening amide groups in self-assembly, gelation, optical and semiconducting properties

Soft Matter ◽  
2019 ◽  
Vol 15 (14) ◽  
pp. 3018-3026 ◽  
Author(s):  
Nibedita Nandi ◽  
Kousik Gayen ◽  
Arindam Banerjee
Keyword(s):  
Amino Acid ◽  
Self Assembly ◽  
Naphthalene Diimide ◽  
Semiconducting Properties

Two isomeric amino-acid containing naphthalene diimide based molecules differ in their respective assembly and the intervening amide groups plays an important role in gelation, optical and semiconducting nature of these molecules.

Mimicking the Function of Eggshell Matrix Proteins: The Role of Multiplets of Charged Amino Acid Residues and Self-Assembly of Peptides in Biomineralization

2005 ◽  
Vol 44 (34) ◽  
pp. 5476-5479 ◽  
Author(s):  
Parayil Kumaran Ajikumar ◽  
Subramanian Vivekanandan ◽  
Rajamani Lakshminarayanan ◽  
Seetharama D. S. Jois ◽  
R. Manjunatha Kini ◽  
...  
Keyword(s):  
Amino Acid ◽  
Self Assembly ◽  
Matrix Proteins ◽  
Amino Acid Residues ◽  
Eggshell Matrix

Clarifying the influence of core amino acid hydrophobicity, secondary structure propensity, and molecular volume on amyloid-β 16–22 self-assembly

2011 ◽  
Vol 7 (2) ◽  
pp. 497-510 ◽  
Author(s):  
F. Timur Senguen ◽  
Todd M. Doran ◽  
Elizabeth A. Anderson ◽  
Bradley L. Nilsson
Keyword(s):  
Amino Acid ◽  
Secondary Structure ◽  
Self Assembly ◽  
Amyloid Β ◽  
Molecular Volume

Mimicking the Function of Eggshell Matrix Proteins: The Role of Multiplets of Charged Amino Acid Residues and Self-Assembly of Peptides in Biomineralization

2005 ◽  
Vol 117 (34) ◽  
pp. 5612-5615 ◽  
Author(s):  
Parayil Kumaran Ajikumar ◽  
Subramanian Vivekanandan ◽  
Rajamani Lakshminarayanan ◽  
Seetharama D. S. Jois ◽  
R. Manjunatha Kini ◽  
...  
Keyword(s):  
Amino Acid ◽  
Self Assembly ◽  
Matrix Proteins ◽  
Amino Acid Residues ◽  
Eggshell Matrix

scholarly journals Unravelling the role of amino acid sequence order in the assembly and function of the amyloid-β core

2019 ◽  
Vol 55 (59) ◽  
pp. 8595-8598 ◽  
Author(s):  
Santu Bera ◽  
Elad Arad ◽  
Lee Schnaider ◽  
Shira Shaham-Niv ◽  
Valeria Castelletto ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Self Assembly ◽  
Amyloid Β ◽  
The Self ◽  
Biological Functions ◽  
The Core ◽  
Recognition Motif ◽  
And Function

Here we report the influence of amino acid sequence order on the self-assembly and biological functions of the core recognition motif of Amyloid β.

Single Amino Acid Based Self-Assemblies of Cysteine and Methionine

2018 ◽  
Author(s):  
Nidhi Gour ◽  
Bharti Koshti ◽  
Chandra Kanth P. ◽  
Dhruvi Shah ◽  
Vivek Shinh Kshatriya ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Self Assembly ◽  
Aromatic Amino Acids ◽  
Neutral Condition ◽  
Single Amino Acid ◽  
Binding Assays ◽  
Human Neuroblastoma ◽  
Cytotoxicity Assays ◽  
First Time

We report for the very first time self-assembly of Cysteine and Methionine to discrenible strucutres under neutral condition. To get insights into the structure formation, thioflavin T and Congo red binding assays were done which revealed that aggregates may not have amyloid like characteristics. The nature of interactions which lead to such self-assemblies was purported by coincubating assemblies in urea and mercaptoethanol. Further interaction of aggregates with short amyloidogenic dipeptide diphenylalanine (FF) was assessed. While cysteine aggregates completely disrupted FF fibres, methionine albeit triggered fibrillation. The cytotoxicity assays of cysteine and methionine structures were performed on Human Neuroblastoma IMR-32 cells which suggested that aggregates are not cytotoxic in nature and thus, may not have amyloid like etiology. The results presented in the manuscript are striking, since to the best of our knowledge,this is the first report which demonstrates that even non-aromatic amino acids (cysteine and methionine) can undergo spontaneous self-assembly to form ordered aggregates.

Directive Effect of Chain Length in Modulating Peptide Nano-assemblies

2020 ◽  
Vol 27 (9) ◽  
pp. 923-929
Author(s):  
Gaurav Pandey ◽  
Prem Prakash Das ◽  
Vibin Ramakrishnan
Keyword(s):  
Electron Microscopy ◽  
Amino Acids ◽  
Light Scattering ◽  
Chain Length ◽  
Self Assembly ◽  
The Self ◽  
Ionic Charge ◽  
Self Assembling ◽  
Biophysical Techniques

Background: RADA-4 (Ac-RADARADARADARADA-NH2) is the most extensively studied and marketed self-assembling peptide, forming hydrogel, used to create defined threedimensional microenvironments for cell culture applications. Objectives: In this work, we use various biophysical techniques to investigate the length dependency of RADA aggregation and assembly. Methods: We synthesized a series of RADA-N peptides, N ranging from 1 to 4, resulting in four peptides having 4, 8, 12, and 16 amino acids in their sequence. Through a combination of various biophysical methods including thioflavin T fluorescence assay, static right angle light scattering assay, Dynamic Light Scattering (DLS), electron microscopy, CD, and IR spectroscopy, we have examined the role of chain-length on the self-assembly of RADA peptide. Results: Our observations show that the aggregation of ionic, charge-complementary RADA motifcontaining peptides is length-dependent, with N less than 3 are not forming spontaneous selfassemblies. Conclusion: The six biophysical experiments discussed in this paper validate the significance of chain-length on the epitaxial growth of RADA peptide self-assembly.

An ESR study of the peroxidase reaction catalyzed by human methaemoglobin and methaemoglobin-haptoglobin complex

1991 ◽  
Vol 56 (4) ◽  
pp. 923-932
Author(s):  
Jana Stejskalová ◽  
Pavel Stopka ◽  
Zdeněk Pavlíček
Keyword(s):  
Hydrogen Peroxide ◽  
Ascorbic Acid ◽  
Amino Acid ◽  
Peroxidase Activity ◽  
Amino Acid Analysis ◽  
Superoxide Radical ◽  
Esr Spectra ◽  
The Other ◽  
Delocalized Electron

The ESR spectra of peroxidase systems of methaemoglobin-ascorbic acid-hydrogen peroxide and methaemoglobin-haptoglobin complex-ascorbic acid-hydrogen peroxide have been measured in the acetate buffer of pH 4.5. For the system with methaemoglobin an asymmetrical signal with g ~ 2 has been observed which is interpreted as the perpendicular region of anisotropic spectrum of superoxide radical. On the other hand, for the system with methaemoglobin-haptoglobin complex the observed signal with g ~ 2 is symmetrical and is interpreted as a signal of delocalized electron. After realization of three repeatedly induced peroxidase processes the ESR signal of the perpendicular part of anisotropic spectrum of superoxide radical is distinctly diminished, whereas the signal of delocalized electron remains practically unchanged. An amino acid analysis of methaemoglobin along with results of the ESR measurements make it possible to derive a hypothesis about the role of haptoglobin in increasing of the peroxidase activity of methaemoglobin.

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