On the temperature-induced coil to globule transition of poly-N-isopropylacrylamide in dilute aqueous solutions.

Abstract:

:Poly-N-isopropylacrylamide (PNIPAM) is a chemical isomer of poly-leucine, having the polar peptide group in the side-chain rather than in the backbone. It has been demonstrated experimentally that PNIPAM dissolved in aqueous solution undergoes a collapse transition from coil to globule on increasing temperature above the θ-point. By a careful reviewing of existing experimental data, we emphasize that such coil to globule collapse has to be considered an intramolecular first-order transition, analogous to the cold renaturation of small globular proteins. The main theoretical approaches to the coil to globule collapse in homopolymers are discussed briefly, and a critical comparison between the existing models is performed. We point out that, as a general result, the coil to globule collapse is expected to be a first-order transition for rigid and semi-rigid macromolecules. Finally, taking advantage of the analogy between the coil to globule collapse of PNIPAM and the cold renaturation of small globular proteins, we try to clarify some important and intriguing aspects of protein thermodynamics. This leads to the conclusion that the amphiphilic nature of polypeptide chain plays the fundamental role for the existence of two temperature-induced conformational transitions.

journal_name

Int J Biol Macromol

authors

Graziano G

doi

10.1016/s0141-8130(99)00122-1

keywords:

subject

Has Abstract

pub_date

2000-03-16 00:00:00

pages

89-97

issue

1

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(99)00122-1

journal_volume

27

pub_type

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