Morphology and aggregation of RADA-16-I peptide Studied by AFM, NMR and molecular dynamics simulations.

Abstract:

:RADA-16-I is a self-assembling peptide which forms biocompatible fibrils and hydrogels. We used molecular dynamics simulations, atomic-force microscopy, NMR spectroscopy, and thioflavin T binding assay to examine size, structure, and morphology of RADA-16-I aggregates. We used the native form of RADA-16-I (H-(ArgAlaAspAla)4 -OH) rather than the acetylated one commonly used in the previous studies. At neutral pH, RADA-16-I is mainly in the fibrillar form, the fibrils consist of an even number of stacked β-sheets. At acidic pH, RADA-16-I fibrils disassemble into monomers, which form an amorphous monolayer on graphite and monolayer lamellae on mica. RADA-16-I fibrils were compared with the fibrils of a similar peptide RLDL-16-I. Thickness of β-sheets measured by AFM was in excellent agreement with the molecular dynamics simulations. A pair of RLDL-16-I β-sheets was thicker (2.3 ± 0.4 nm) than a pair of RADA-16-I β-sheets (1.9 ± 0.1 nm) due to the volume difference between alanine and leucine residues.

journal_name

Biopolymers

journal_title

Biopolymers

authors

Bagrov D,Gazizova Y,Podgorsky V,Udovichenko I,Danilkovich A,Prusakov K,Klinov D

doi

10.1002/bip.22755

subject

Has Abstract

pub_date

2016-01-01 00:00:00

pages

72-81

issue

1

eissn

0006-3525

issn

1097-0282

journal_volume

106

pub_type

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