An overlooked UV spectroscopic tool for sensing coil-to- ...

Published by: Elsevier

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Highlights

• •

  Coil-to-helix conformational transitions of disordered peptide/protein sequences is accompanied by far-UV hypochromism.

• •

  Conversely, unfolding of helical polypeptide chains results in hyperchromism in the far-UV absorption region.

• •

  Detection of UV hypo- and hyperchromism of disordered and helical sequences offers a simple, easy-to-use and cost-effective method for sensing folding and unfolding events prompted by various effects.

Abstract

A simple spectrophotometric approach is proposed for sensing coil-to-helix and helix-to-coil conformational transitions of intrinsically disordered and folded peptide/protein sequences. Helix formation induced by a variety of physico-chemical factors results in a substantial intensity reduction (hypochromism) of the intense far-UV absorption band associated with the π-π* transition of amide chromophores. Conversely, the same band exhibits intensity increase (hyperchromism) as the consequence of unfolding events. This method, faded into obscurity several decades ago, may obtain widespread applications in the field of protein science.

Keywords

Far-ultraviolet absorption spectroscopy

;

Helical folding

;

Hyperchromism

;

Hypochromism

;

Intrinsic disorder

;

Peptide

;

Protein

;

Random coil

Abbreviations

IDP,

intrinsically disordered protein

;

IDPR,

intrinsically disordered protein region

;

PGA,

poly-l-glutamic acid

;

TFE,

2,2,2-trifluoroethanol

;

UV/VIS,

ultraviolet/visible

;

CD,

circular dichroism

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© 2021 The Author. Published by Elsevier Inc.