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Lattice model for polymer hydration: collapse of poly( N ‐isopropylacrylamide)
Author(s) -
Bruscolini Pierpaolo,
Buzano Carla,
Pelizzola Alessandro,
Pretti Marco
Publication year - 2002
Publication title -
macromolecular symposia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.257
H-Index - 76
eISSN - 1521-3900
pISSN - 1022-1360
DOI - 10.1002/1521-3900(200205)181:1<261::aid-masy261>3.0.co;2-z
Subject(s) - monomer , poly(n isopropylacrylamide) , polymer , thermodynamics , aqueous solution , chemical physics , globular protein , entropy (arrow of time) , materials science , chemistry , polymer chemistry , crystallography , copolymer , physics , composite material
Poly(N‐isopropylacrylamide) (PNIPAM) in dilute aqueous solution undergoes a collapse transition from coil to globule on increasing temperature. Such coil‐to‐globule collapse is usually considered analogous to the cold renaturation of small globular proteins. In this paper we propose a theoretical approach that is able to reproduce, in a semi‐quantitative way, the unusual behavior of PNIPAM, and the observed thermodynamic properties. The procedure is based on two main steps: (i) the characterization of single monomer hydration thermodynamics, interpreted by a balance between the removal of monomer‐monomer interactions and the addition of water‐monomer interactions, and (ii) a simplified analysis of a lattice self‐avoiding walk (SAW) model, which allows to account for the configurational entropy in a controlled way, and hence to relate the microscopic interactions to the “macroscopic” behavior of the polymer chain. The results show that the temperature dependence and magnitude of the interaction parameters that best fit experimental data validate a recently proposed qualitative interpretation of the mechanism of collapse transition for PNIPAM. The latter result turns out to be relevant to support the analogy with the cold renaturation of small globular proteins, and to clarify some important aspects of protein thermodynamics.