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Protein & Peptide Letters

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ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

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Letter Article

Directive Effect of Chain Length in Modulating Peptide Nano-assemblies

Author(s): Gaurav Pandey, Prem Prakash Das and Vibin Ramakrishnan*

Volume 27, Issue 9, 2020

Page: [923 - 929] Pages: 7

DOI: 10.2174/0929866527666200224114627

Price: $65

Abstract

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.

Keywords: Functional peptides, microenvironments, biophysical techniques, nanofibers, peptide self-assembly, RADA peptide.

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